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2008
Basova LV, Tiktopulo EI, Kutyshenko VP, Mauk AG, Bychkova VE.
Phospholipid membranes affect tertiary structure of the soluble cytochrome b(5) heme-binding domain. Biochim Biophys Acta. 2008 Apr;1778(4):1015-26. Epub 2008 Jan 17. PubMed
Finkelstein A.V., Ivankov D.N., Garbuzynskiy S.O., Galzitskaya O.V.
Protein structure and its folding rate. In "Mathematical Modelling of Biosystems" (Eds.: R.P. Mondaini, P.M. Pardalos). Springer Verlag, in press.
Galzitskaya OV, Reifsnyder DC, Bogatyreva NS, Ivankov DN, Garbuzynskiy SO.
More compact protein globules exhibit slower folding rates. Proteins. 2008 Feb 1;70(2):329-32. PubMed
Garbuzynskiy SO, Kondratova MS.
Structural features of protein folding nuclei. FEBS Lett. 2008 Mar 5;582(5):768-72. Epub 2008 Feb 5. PubMed
Melnik BS, Marchenkov VV, Evdokimov SR, Samatova EN, Kotova NV.
Multy-state protein: Determination of carbonic anhydrase free-energy landscape. Biochem Biophys Res Commun. 2008 May 2;369(2):701-6. Epub 2008 Feb 29. PubMed
2007
Baryshnikova EN, Balobanov VA, Katina NS, Mel'nik BS, Dolgikh DA, Semisotnov GV, Bychkov VE.
[Equilibrium unfolding of mutant apomyoglobins with substitutions of conserved nonfunctional residues by alanine] Mol Biol (Mosk). 2007 Jul-Aug;41(4):674-80. Russian. PubMed
Dovidchenko NV, Lobanov MY, Galzitskaya OV.
Prediction of number and position of domain boundaries in multi-domain proteins by use of amino acid sequence alone. Curr Protein Pept Sci. 2007 Apr;8(2):189-95. Review. PubMed
Finkelstein AV, Ivankov DN, Garbuzynskiy SO, Galzitskaya OV.
Understanding the folding rates and folding nuclei of globular proteins. Curr Protein Pept Sci. 2007 Dec;8(6):521-36. Review. PubMed
Finkelstein AV.
Average and extreme multi-atom Van der Waals interactions: Strong coupling of multi-atom Van der Waals interactions with covalent bonding. Chem Cent J. 2007 Jul 30;1:21. PubMed
Galzitskaya O.V., Garbuzynskiy S.O., Lobanov M.Yu.
Expected packing density allows prediction of both amyloidogenic and disordered regions in protein chains. Journal of Physics: Condensed Matter, 2007, v.19 (28), 285225 (15 pp).
Gliakina AV, Lobanov AV, Galzitskaia OV.
[Search for structural factors responsible for the stability of proteins from thermophilic organisms]. Mol Biol (Mosk). 2007 Jul-Aug;41(4):681-7. Russian. PubMed
Glyakina AV, Garbuzynskiy SO, Lobanov MY, Galzitskaya OV.
Different packing of external residues can explain differences in the thermostability of proteins from thermophilic and mesophilic organisms. Bioinformatics. 2007 Sep 1;23(17):2231-8. Epub 2007 Jun 28. PubMed
Rodikova EA, Kovalevskiy OV, Mayorov SG, Budarina ZI, Marchenkov VV, Melnik BS, Leech AP, Nikitin DV, Shlyapnikov MG, Solonin AS.
Two HlyIIR dimers bind to a long perfect inverted repeat in the operator of the hemolysin II gene from Bacillus cereus. FEBS Lett. 2007 Mar 20;581(6):1190-6. Epub 2007 Feb 28. PubMed
Ibryashkina EM, Zakharova MV, Baskunov VB, Bogdanova ES, Nagornykh MO, Den'mukhamedov MM, Melnik BS, Kolinski A, Gront D, Feder M, Solonin AS, Bujnicki JM.
Type II restriction endonuclease R.Eco29kI is a member of the GIY-YIG nuclease superfamily. BMC Struct Biol. 2007 Jul 12;7:48. PubMed
Savitski MM, Kjeldsen F, Nielsen ML, Garbuzynskiy SO, Galzitskaya OV, Surin AK, Zubarev RA.
Backbone carbonyl group basicities are related to gas-phase fragmentation of peptides and protein folding. Angew Chem Int Ed Engl. 2007;46(9):1481-4. No abstract available. PubMed
2006
Bogatyreva NS, Finkelstein AV, Galzitskaya OV.
Trend of amino acid composition of proteins of different taxa. J Bioinform Comput Biol. 2006 Apr;4(2):597-608. PubMed
Finkelstein AV, Ivankov DN, Dykhne AM.
Energy barrier for an ion crossing an intra-membrane channel. 2006. ArXiv:physics/0612139 PDF
Galzitskaia OV, Dovidchenko NV, Lobanov MIu, Garbuzinskii SA.
[Prediction of protein domain boundaries based on statistics of appearance of amino acid residues]. Mol Biol (Mosk). 2006 Jan-Feb;40(1):111-21. Russian. PubMed
Galzitskaya OV, Garbuzynskiy SO.
Entropy capacity determines protein folding. Proteins. 2006 Apr 1;63(1):144-54. PubMed
Galzitskaya OV, Garbuzynskiy SO, Lobanov MY.
FoldUnfold: web server for the prediction of disordered regions in protein chain. Bioinformatics. 2006 Oct 4; [Epub ahead of print] PubMed
Galzitskaya OV, Garbuzynskiy SO, Lobanov MY.
Is it possible to predict amyloidogenic regions from sequence alone? J Bioinform Comput Biol. 2006 Apr;4(2):373-88. PubMed
Galzitskaia OV, Garbuzinskii SA, Lobanov MIu.
[A search for amyloidogenic regions in protein chain]. Mol Biol (Mosk). 2006 Sep-Oct;40(5):910-8. Russian. PubMed
Galzitskaia OV, Garbuzinskii SA.
[Optimal relationship between average conformational entropy and average energy of interactions between residues for fast protein folding]. Biofizika. 2006 Jul-Aug;51(4):622-32. Russian. PubMed
Galzitskaia OV, Garbuzinskii SA, Lobanov MIu.
[Prediction of natively unfolded regions in protein chain] Mol Biol (Mosk). 2006 Mar-Apr;40(2):341-8. Russian. PubMed
Kovalevskiy OV, Lebedev AA, Surin AK, Solonin AS, Antson AA.
Crystal structure of Bacillus cereus HlyIIR, a transcriptional regulator of the gene for pore-forming toxin hemolysin II. J Mol Biol. 2007 Jan 19;365(3):825-34. Epub 2006 Oct 26. PubMed
Marchenko NIu, Marchenkov VV, Kaisheva AL, Kashparov IA, Kotova NV, Kaliman PA, Semisotnov GV.
Affinity chromatography of GroEL chaperonin based on denatured proteins: role of electrostatic interactions in regulation of GroEL affinity for protein substrates. Biochemistry (Mosc). 2006 Dec;71(12):1357-64. PubMed
2005
Basova LV, Tiktopulo EI, Bychkova VE.
Model phospholipid membranes affect the holomyoglobin structure: conformational changes at pH 6.2. Mol Biol (Mosk). 2005 Jan-Feb;39(1):120-8. Russian. PubMed
Baryshnikova EN, Melnik BS, Finkelstein AV, Semisotnov GV, Bychkova VE.
Three-state protein folding: experimental determination of free-energy profile. Protein Sci. 2005 Oct;14(10):2658-67. PubMed
Baryshnikova EN, Mel'nik BS, Semisotnov GV, Bychkova VE.
Investigation of folding/unfolding kinetics of apomyoglobin. Mol Biol (Mosk). 2005 Nov-Dec;39(6):1008-16. Russian. PubMed
Baryshnikova EN, Sharanov MG, Kashparov IA, Il'ina NB, Bychkova VE.
Investigation of apomyoglobin stability depending on urea and temperature at two different pH values. Mol Biol (Mosk). 2005 Mar-Apr;39(2):330-5. Russian. PubMed
Galzitskaya O.V., Garbuzynskiy S.O., Finkelstein A.V.
Theoretical study of protein folding: outlining folding nuclei and estimation of protein folding rates. Journal of Physics: Condensed Matter, 2005, v.17 (18), pp. S1539-S1551.
Garbuzinskii SA, Finkel'shtein AV, Galzitskaia OV.
[On prediction of folding nuclei in globular proteins]. Mol Biol (Mosk). 2005 Nov-Dec;39(6):1032-41. Russian. PubMed
Garbuzynskiy SO, Melnik BS, Lobanov MY, Finkelstein AV, Galzitskaya OV.
Comparison of X-ray and NMR structures: is there a systematic difference in residue contacts between X-ray- and NMR-resolved protein structures? Proteins. 2005 Jul 1;60(1):139-47. PubMed
Mel'nik BS, Garbuzinskii SA, Lobanov MIu, Galzitskaia OV.
[The difference between protein structures that are obtained by X-ray analysis and magnetic resonance spectroscopy]. Mol Biol (Mosk). 2005 Jan-Feb;39(1):129-38. Russian. PubMed
Morozova OB, Hore PJ, Bychkova VE, Sagdeev RZ, Yurkovskaya AV.
Time-resolved CIDNP study of non-native states of bovine and human alpha-lactalbumins. J Phys Chem B Condens Matter Mater Surf Interfaces Biophys. 2005 Mar 31;109(12):5912-8. PubMed
Финкельштейн А.В., Иванков Д.Н., Галзитская О.В.
Предсказание скоростей и ядер сворачивания глобулярных белков на основе теории их самоорганизации. Успехи биологической химии, 2005, 45: 3-36.
2004
Basov LV, Tiktopulo EI, Kashparov IA, Bychkova VE.
Conformational status of apomyoglobin in the presence of phospholipid vesicles at neutral pH. Mol Biol (Mosk). 2004 Mar-Apr;38(2):323-32. Russian. PubMed
Garbuzynskiy SO, Finkelstein AV, Galzitskaya OV.
Outlining folding nuclei in globular proteins. J Mol Biol. 2004 Feb 13;336(2):509-25. PubMed
Garbuzynskiy SO, Lobanov MY, Galzitskaya OV.
To be folded or to be unfolded? Protein Sci. 2004 Nov;13(11):2871-7. PubMed
Gorokhovatsky AY, Marchenkov VV, Rudenko NV, Ivashina TV, Ksenzenko VN, Burkhardt N, Semisotnov GV, Vinokurov LM, Alakhov YB.
Fusion of Aequorea victoria GFP and aequorin provides their Ca(2+)-induced interaction that results in red shift of GFP absorption and efficient bioluminescence energy transfer. Biochem Biophys Res Commun. 2004 Jul 30;320(3):703-11. PubMed
Ivankov DN, Finkelstein AV.
Prediction of protein folding rates from the amino acid sequence-predicted secondary structure. Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):8942-4. Epub 2004 Jun 07. PubMed
Krieger E, Darden T, Nabuurs SB, Finkelstein A, Vriend G.
Making optimal use of empirical energy functions: Force-field parameterization in crystal space. Proteins. 2004 Aug 18;57(4):678-683. PubMed
Sunyaev SR, Bogopolsky GA, Oleynikova NV, Vlasov PK, Finkelstein AV, Roytberg MA.
From analysis of protein structural alignments toward a novel approach to align protein sequences. Proteins. 2004 Feb 15;54(3):569-82. PubMed
Suzuki S, Galzitskaya OV, Mitomo D, Higo J.
General Dynamic Properties of A{beta}12-36 Amyloid Peptide Involved in Alzheimer's Disease from Unfolding Simulation. J Biochem (Tokyo). 2004 Nov;136(5):583-594. PubMed
Torta F, Dyuysekina AE, Cavazzini D, Fantuzzi A, Bychkova VE, Rossi GL.
Solvent-induced ligand dissociation and conformational states of Cellular Retinol-Binding Protein type I. Biochim Biophys Acta. 2004 Dec 1;1703(1):21-9. PubMed
2003
Galzitskaya OV, Garbuzynskiy SO, Ivankov DN, Finkelstein AV.
Chain length is the main determinant of the folding rate for proteins with three-state folding kinetics. Proteins. 2003 May 1;51(2):162-6. PubMed
Galzitskaya OV, Melnik BS.
Prediction of protein domain boundaries from sequence alone. Protein Sci. 2003 Apr;12(4):696-701. PubMed
Gorokhovatsky AY, Rudenko NV, Marchenkov VV, Skosyrev VS, Arzhanov MA, Burkhardt N, Zakharov MV, Semisotnov GV, Vinokurov LM, Alakhov YB.
Homogeneous assay for biotin based on Aequorea victoria bioluminescence resonance energy transfer system. Anal Biochem. 2003 Feb 1;313(1):68-75. PubMed
Ikeda K, Galzitskaya OV, Nakamura H, Higo J.
beta-Hairpins, alpha-helices, and the intermediates among the secondary structures in the energy landscape of a peptide from a distal beta-hairpin of SH3 domain. J Comput Chem. 2003 Feb;24(3):310-8. PubMed
Ivankov DN, Garbuzynskiy SO, Alm E, Plaxco KW, Baker D, Finkelstein AV.
Contact order revisited: influence of protein size on the folding rate. Protein Sci. 2003 Sep;12(9):2057-62. PubMed
Marchenko NIu, Marchenkov VV, Kotova NV, Semisotnov GV, Bulankina NI, Kaliman PA.
Effect of ADP and GroES on interaction of molecular chaperonin GroEL with non-native lysozyme. Ukr Biokhim Zh. 2003 May-Jun;75(3):88-94. Russian. PubMed
2002
Basova LV, Il'ina NB, Vasilenko KS, Tiktopulo EI, Bychkova VE.
Conformational states of the water-soluble fragment of cytochrome b5. I. pH-induced denaturation. Mol Biol (Mosk). 2002 Sep-Oct;36(5):891-900. Russian. PubMed
Finkelstein AV.
Cunning simplicity of a hierarchical folding. J Biomol Struct Dyn. 2002 Dec;20(3):311-3. PubMed
Galzitskaya OV, Higo J, Finkelstein AV.
Alpha-helix and beta-hairpin Folding from experiment, analytical theory and molecular dynamics simulations. Curr Protein Pept Sci. 2002 Apr;3(2):191-200. Review. PubMed
Kister AE, Finkelstein AV, Gelfand IM.
Common features in structures and sequences of sandwich-like proteins. Proc Natl Acad Sci U S A. 2002 Oct 29;99(22):14137-41. Epub 2002 Oct 16. PubMed
2001
Bogatyreva NS, Finkelstein AV.
Cunning simplicity of protein folding landscapes. Protein Eng. 2001 Aug;14(8):521-3. PubMed
Galzitskaya OV, Ivankov DN, Finkelstein AV.
Folding nuclei in proteins. FEBS Lett. 2001 Feb 2;489(2-3):113-8. Review. PubMed
Galzitskaya OV, Ivankov DN, Finkelstein AV.
Kinetics of folding nuclei formation in proteins. Mol Biol (Mosk). 2001 Jul-Aug;35(4):708-17. Review. Russian. PubMed
Ivankov DN, Finkelstein AV.
Theoretical study of a landscape of protein folding-unfolding pathways. Folding rates at midtransition. Biochemistry. 2001 Aug 21;40(33):9957-61. PubMed
Latypov RF, Dolgikh DA, Kirpichnikov MP, Ptitsyn OB, Roder H.
Y97V substitution in the horse cytochrome c causes accumulation of the equilibrium intermediate. Biofizika. 2001 Jan-Feb;46(1):46-52. Russian. PubMed
Lindberg MO, Tangrot J, Otzen DE, Dolgikh DA, Finkelstein AV, Oliveberg M.
Folding of circular permutants with decreased contact order: general trend balanced by protein stability. J Mol Biol. 2001 Dec 7;314(4):891-900. PubMed
Szilagyi AN, Kotova NV, Semisotnov GV, Vas M.
Incomplete refolding of a fragment of the N-terminal domain of pig muscle 3-phosphoglycerate kinase that lacks a subdomain. Comparison with refolding of the complementary C-terminal fragment. Eur J Biochem. 2001 Mar;268(6):1851-60. PubMed
2000
Galzitskaya OV, Skoogarev AV, Ivankov DN, Finkelstein AV.
Folding nuclei in 3D protein structures. Pac Symp Biocomput. 2000;:131-42. PubMed
Galzitskaya OV, Surin AK, Nakamura H.
Optimal region of average side-chain entropy for fast protein folding. Protein Sci. 2000 Mar;9(3):580-6. PubMed
Mirny LA, Finkelstein AV, Shakhnovich EI.
Statistical significance of protein structure prediction by threading. Proc Natl Acad Sci U S A. 2000 Aug 29;97(18):9978-83. PubMed
Reva BA, Finkelstein AV, Skolnick J.
Derivation and testing residue-residue mean-force potentials for use in protein structure recognition. Methods Mol Biol. 2000;143:155-74. PubMed
Rykunov DS, Lobanov MY, Finkelstein AV.
Search for the most stable folds of protein chains: III. Improvement in fold recognition by averaging over homologous sequences and 3D structures. Proteins. 2000 Aug 15;40(3):494-501. PubMed
Tcherkasskaya O, Bychkova VE, Uversky VN, Gronenborn AM.
Multisite fluorescence in proteins with multiple tryptophan residues. Apomyoglobin natural variants and site-directed mutants. J Biol Chem. 2000 Nov 17;275(46):36285-94. PubMed
Tcherkasskaya O, Ptitsyn OB, Knutson JR.
Nanosecond dynamics of tryptophans in different conformational states of apomyoglobin proteins. Biochemistry. 2000 Feb 22;39(7):1879-89. PubMed
Timchenko AA, Melnik BS, Kihara H, Kimura K, Semisotnov GV.
GroES co-chaperonin small-angle X-ray scattering study shows ring orifice increase in solution. FEBS Lett. 2000 Apr 14;471(2-3):211-4. PubMed
1999
Galzitskaya O, Caflisch A.
Solution conformation of phakellistatin 8 investigated by molecular dynamics simulations. J Mol Graph Model. 1999 Feb;17(1):19-27. PubMed
Galzitskaya OV, Finkelstein AV.
A theoretical search for folding/unfolding nuclei in three-dimensional protein structures. Proc Natl Acad Sci U S A. 1999 Sep 28;96(20):11299-304. PubMed
Ptitsyn OB, Finkel'shtein AV, Dobson CM.
Self-organization of protein structures--a bridge between physics and biology. Mol Biol (Mosk). 1999 Nov Dec;33(6):1012-5. Review. Russian. PubMed
Ptitsyn OB, Ting KL.
Non-functional conserved residues in globins and their possible role as a folding nucleus. J Mol Biol. 1999 Aug 20;291(3):671-82. PubMed
Ptitsyn OB.
Protein evolution and protein folding: non-functional conserved residues and their probable role. Pac Symp Biocomput. 1999;:494-504. PubMed
Reva BA, Skolnick J, Finkelstein AV.
Averaging interaction energies over homologs improves protein fold recognitionin gapless threading. Proteins. 1999 May 15;35(3):353-9. PubMed
Surin AK, Kotova NV, Marchenkova SIu, Marchenkov VV, Semisotnov GV.
Monomeric form of the molecular chaperone GroEL: structure, stability, and oligomerization. Bioorg Khim. 1999 May;25(5):358-64. Russian. PubMed
Tcherkasskaya O, Ptitsyn OB.
Direct energy transfer to study the 3D structure of non-native proteins: AGH complex in molten globule state of apomyoglobin. Protein Eng. 1999 Jun;12(6):485-90. PubMed
Tcherkasskaya O, Ptitsyn OB.
Molten globule versus variety of intermediates: influence of anions on pH-denatured apomyoglobin. FEBS Lett. 1999 Jul 23;455(3):325-31. PubMed
1998
Afasizheva IIu, Dolgikh DA, Abdullaev ZKh, Latypov RF, Tiktopulo EI, Uverskii VN, Ptitsyn OB, Kirpichnikov MP.
Effect of a biologically active interferon fragment on the structure of the synthetic protein carrier. Biofizika. 1998 May-Jun;43(3):384-91. Russian. PubMed
Aphasizheva IY, Dolgikh DA, Abdullaev ZK, Uversky VN, Kirpichnikov MP, Ptitsyn OB.
Can grafting of an octapeptide improve the structure of a de novo protein? FEBS Lett. 1998 Mar 20;425(1):101-4. PubMed
Arai M, Ikura T, Semisotnov GV, Kihara H, Amemiya Y, Kuwajima K.
Kinetic refolding of beta-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy. J Mol Biol. 1998 Jan 9;275(1):149-62. PubMed
Badretdinov AYa, Finkelstein AV.
How homologs can help to predict protein folds even though they cannot be predicted for individual sequences. J Comput Biol. 1998 Fall;5(3):369-76. PubMed
Bychkova VE, Dujsekina AE, Fantuzzi A, Ptitsyn OB, Rossi GL.
Release of retinol and denaturation of its plasma carrier, retinol-binding protein.Fold Des. 1998;3(4):285-91. PubMed
Diuisekina AE, Bychkova VE, Fantuzzi A, Rossi GL, Ptitsin OB.
Release of hydrophobic ligand from retinol-binding protein under conditions mimicked the membrane field. Mol Biol (Mosk). 1998 Jan-Feb;32(1):133-40. Russian. PubMed
Galzitskaya O, Finkelstein AV.
Folding rate dependence on the chain length of RNA-like heteropolymers. Fold Des. 1998;3(2):69-78. PubMed
Keskin O, Bahar I, Badretdinov AY, Ptitsyn OB, Jernigan RL.
Empirical solvent-mediated potentials hold for both intra-molecular and inter-molecular inter-residue interactions. Protein Sci. 1998 Dec;7(12):2578-86. PubMed
Korotkov KV, Plotnikov AN, Motuz LP, Vasilenko KS, Semisotnov GV, Alakhov IuB.
Characteristics of N-terminal 60-kDa fragment of elongation factor 2. Bioorg Khim. 1998 Mar;24(3):171-4. Russian. PubMed
Ptitsyn OB.
Protein folding and protein evolution: common folding nucleus in different subfamilies of c-type cytochromes? J Mol Biol. 1998 May 8;278(3):655-66. PubMed
Ptitsyn OB.
Protein folding: nucleation and compact intermediates. Biochemistry (Mosc). 1998 Apr;63(4):367-73. Review. PubMed
Reva BA, Finkelstein AV, Skolnick J.
What is the probability of a chance prediction of a protein structure with an rmsd of 6 A? Fold Des. 1998;3(2):141-7. PubMed
Reva BA, Rykunov DS, Finkelstein AV, Skolnick J.
Optimization of protein structure on lattices using a self-consistent field approach. J Comput Biol. 1998 Fall;5(3):531-8. PubMed
Yakhnin AV, Vinokurov LM, Surin AK, Alakhov YB.
Green fluorescent protein purification by organic extraction. Protein Expr Purif. 1998 Dec;14(3):382-6. PubMed
1997
Abdullaev ZK, Latypov RF, Badretdinov AY, Dolgikh DA, Finkelstein AV, Uversky VN, Kirpichnikov MP.
S6 permutein shows that the unusual target topology is not responsible for the absence of rigid tertiary structure in de novo protein albebetin. FEBS Lett. 1997 Sep 8;414(2):243-6. PubMed
Dobson CM, Ptitsyn OB.
Folding and binding. From theory to therapy. Curr Opin Struct Biol. 1997 Feb;7(1):1-2. PubMed
Finkelstein AV, Badretdinov AYa.
Rate of protein folding near the point of thermodynamic equilibrium between the coil and the most stable chain fold. Fold Des. 1997;2(2):115-21. Erratum in: Fold Des 1998;3(1):67. PubMed
Finkelstein AV.
Can protein unfolding simulate protein folding? Protein Eng. 1997 Aug;10(8):843-5. PubMed
Finkelstein AV.
Protein structure: what is it possible to predict now? Curr Opin Struct Biol. 1997 Feb;7(1):60-71. Review. PubMed
Galzitskaya O, Finkelstein AV.
Folding rate dependence on the chain length of RNA-like heteropolymers. Fold Des. 1998;3(2):69-78. PubMed
Galzitskaya OV.
Geometrical factor and physical reasons for its influence on the kinetic and thermodynamic properties of RNA-like heteropolymers. Fold Des. 1997;2(3):193-201. PubMed
Kharakoz DP, Bychkova VE.
Molten globule of human alpha-lactalbumin: hydration, density, and compressibility of the interior. Biochemistry. 1997 Feb 18;36(7):1882-90. PubMed
Plotnikov AN, Vasilenko KS, Kirkitadze MD, Kotova NV, Motuz LP, Korotkov KV, Semisotnov GV, Alakhov IuB.
Biosynthesis and conformational state of 17-kDa and 27-kDa N-terminal fragments of elongation factor EF-2 in solution. Bioorg Khim. 1996 Jul;22(7):489-502. Russian. PubMed
Reva BA, Finkelstein AV, Sanner M, Olson AJ, Skolnick J.
Recognition of protein structure on coarse lattices with residue-residue energy functions. Protein Eng. 1997 Oct;10(10):1123-30. PubMed
Reva BA, Finkelstein AV, Sanner MF, Olson AJ.
Accurate mean-force pairwise-residue potentials for discrimination of protein folds. Pac Symp Biocomput. 1997;:373-84. PubMed
Reva BA, Finkelstein AV, Sanner MF, Olson AJ.
Residue-residue mean-force potentials for protein structure recognition. Protein Eng. 1997 Aug;10(8):865-76. PubMed
Semisotnov GV, Kihara H, Kotova NV, Kimura K, Amemiya Y, Wakabayashi K, Serdyuk IN, Timchenko AA, Chiba K, Nikaido K, Ikura T, Kuwajima K.
Protein globularization during folding. A study by synchrotron small-angle X-ray scattering. J Mol Biol. 1996 Oct 4;262(4):559-74. PubMed
Surin AK, Kotova NV, Kashparov IA, Marchenkov VV, Marchenkova SYu, Semisotnov GV.
Ligands regulate GroEL thermostability. FEBS Lett. 1997 Apr 1;405(3):260-2. PubMed
Surin AK, Kotova NV, Marchenkova SIu, Sokolovskii IV, Rodionova NA, Iaklichkin SIu, Semisotnov GV.
Denatured transitions of the molecular chaperone GroEL from Escherichia coli. Bioorg Khim. 1997 Apr;23(4):251-6. Russian. PubMed
Timchenko AA, Galzitskaya OV, Serdyuk IN.
Roughness of the globular protein surface: analysis of high resolution X-ray data. Proteins. 1997 Jun;28(2):194-201. PubMed
Uverskii VN, Ptitsyn OB.
Three-stage equilibrium unfolding of small globular proteins by denaturing agents. II. Beta-lactamase and general model. Mol Biol (Mosk). 1996 Sep-Oct;30(5):1135-43. Russian. PubMed
Uversky VN, Winter S, Galzitskaya OV, Kittler L, Lober G.
Hyperphosphorylation induces structural modification of tau-protein. FEBS Lett. 1998 Nov 13;439(1-2):21-5. PubMed
1996
Bychkova VE, Dujsekina AE, Klenin SI, Tiktopulo EI, Uversky VN, Ptitsyn OB.
Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface. Biochemistry. 1996 May 14;35(19):6058-63. PubMed
Dolgikh DA, Kirpichnikov MP, Ptitsyn OB, Chemeris VV.
Protein engineering of artificial proteins. Mol Biol (Mosk). 1996 Mar-Apr;30(2):261-72. Review. Russian. PubMed
Finkelstein AV, Reva BA.
Search for the most stable folds of protein chains: I. Application of a self-consistent molecular field theory to a problem of protein three-dimensional structure prediction. Protein Eng. 1996 May;9(5):387-97. PubMed
Kirkitadze MD, Surin AK, Potekhin SA.
Denatured state of lysozyme in dimethyl sulfoxide. Bioorg Khim. 1996 Jan;22(1):20-3. Russian. PubMed
Ptitsyn OB.
A determinable but unresolved problem. FASEB J. 1996 Jan;10(1):3-4. Review. PubMed
Reva BA, Finkelstein AV, Rykunov DS, Olson AJ.
Building self-avoiding lattice models of proteins using a self-consistent field optimization. Proteins. 1996 Sep;26(1):1-8. PubMed
Reva BA, Finkelstein AV, Sanner MF, Olson AJ.
Adjusting potential energy functions for lattice models of chain molecules. Proteins. 1996 Jul;25(3):379-88. PubMed
Reva BA, Finkelstein AV.
Search for the most stable folds of protein chains: II. Computation of stable architectures of beta-proteins using a self-consistent molecular field theory. Protein Eng. 1996 May;9(5):399-411. PubMed
Uverskii VN, Ptitsyn OB.
Three-stage equilibrium unfolding of small globular proteins by denaturing agents. I. Carboanhydrase B. Mol Biol (Mosk). 1996 Sep-Oct;30(5):1124-34. Russian. PubMed
Uversky VN, Ptitsyn OB.
All-or-none solvent-induced transitions between native, molten globule and unfolded states in globular proteins. Fold Des. 1996;1(2):117-22. PubMed
Uversky VN, Ptitsyn OB.
Further evidence on the equilibrium "pre-molten globule state": four-state guanidinium chloride-induced unfolding of carbonic anhydrase B at low temperature. J Mol Biol. 1996 Jan 12;255(1):215-28. PubMed
1995
Bychkova VE, Ptitsyn OB.
The functional state of denatured proteins: the principles of modelling and the first results. Tsitologiia. 1995;37(12):1238-50. Review. Russian. PubMed
Bychkova VE, Ptitsyn OB.
Folding intermediates are involved in genetic diseases? FEBS Lett. 1995 Feb 6;359(1):6-8. PubMed
Finkelstein AV, Badretdinov AYa, Gutin AM.
Why do protein architectures have Boltzmann-like statistics? Proteins. 1995 Oct;23(2):142-50. PubMed
Finkelstein AV, Gutin AM, Badretdinov AY.
Perfect temperature for protein structure prediction and folding. Proteins. 1995 Oct;23(2):151-62. PubMed
Finkelstein AV, Gutin AM, Badretdinov AYa.
Boltzmann-like statistics of protein architectures. Origins and consequences. Subcell Biochem. 1995;24:1-26. Review. PubMed
Finkelstein AV.
Predicted beta-structure stability parameters under experimental test. Protein Eng. 1995 Feb;8(2):207-9. PubMed
Galzitskaya OV, Finkelstein AV.
Folding of chains with random and edited sequences: similarities and differences. Protein Eng. 1995 Sep;8(9):883-92. PubMed
Ptitsyn OB, Bychkova VE, Uversky VN.
Kinetic and equilibrium folding intermediates. Philos Trans R Soc Lond B Biol Sci. 1995 Apr 29;348(1323):35-41. PubMed
Ptitsyn OB.
How the molten globule became. Trends Biochem Sci. 1995 Sep;20(9):376-9. Review. PubMed
Ptitsyn OB.
Molten globule and protein folding. Adv Protein Chem. 1995;47:83-229. Review. PubMed
Ptitsyn OB.
Structures of folding intermediates. Curr Opin Struct Biol. 1995 Feb;5(1):74-8. Review. PubMed
Reva BA, Rykunov DS, Olson AJ, Finkelstein AV.
Constructing lattice models of protein chains with side groups. J Comput Biol. 1995 Winter;2(4):527-35. PubMed
Rykunov DS, Reva BA, Finkelstein AV.
Accurate general method for lattice approximation of three-dimensional structure of a chain molecule. Proteins. 1995 Jun;22(2):100-9. PubMed
1994
Chemeris VV, Dolgikh DA, Fedorov AN, Finkelstein AV, Kirpichnikov MP, Uversky VN, Ptitsyn OB.
A new approach to artificial and modified proteins: theory-based design, synthesis in a cell-free system and fast testing of structural properties by radiolabels. Protein Eng. 1994 Aug;7(8):1041-52. PubMed
Ptitsyn OB, Uversky VN.
The molten globule is a third thermodynamical state of protein molecules. FEBS Lett. 1994 Mar 14;341(1):15-8. PubMed
Ptitsyn OB.
Kinetic and equilibrium intermediates in protein folding. Protein Eng. 1994 May;7(5):593-6. Review. PubMed
Uversky VN, Ptitsyn OB.
"Partly folded" state, a new equilibrium state of protein molecules: four-state guanidinium chloride-induced unfolding of beta-lactamase at low temperature.Biochemistry. 1994 Mar 15;33(10):2782-91. PubMed
1993
Bychkova VE, Ptitsyn OB.
The state of unfolded globules of protein molecules is more quickly becoming a rule, rather than an exception. Biofizika. 1993 Jan-Feb;38(1):58-66. Review. Russian. PubMed
Finkelstein AV, Gutun AM, Badretdinov AYa.
Why are the same protein folds used to perform different functions? FEBS Lett. 1993 Jun 28;325(1-2):23-8. Review. PubMed
Finkelstein AV, Nakamura H.
Weak points of antiparallel beta-sheets. How are they filled up in globular proteins? Protein Eng. 1993 Jun;6(4):367-72. PubMed
Finkelstein AV, Roytberg MA.
Computation of biopolymers: a general approach to different problems. Biosystems. 1993;30(1-3):1-19. PubMed
Kuwajima K, Semisotnov GV, Finkelstein AV, Sugai S, Ptitsyn OB.
Secondary structure of globular proteins at the early and the final stages in protein folding. FEBS Lett. 1993 Nov 22;334(3):265-8. Erratum in: FEBS Lett 1993 Dec 20;336(1):190. PubMed
Ptitsyn OB, Zanotti G, Denesyuk AL, Bychkova VE.
Mechanism of pH-induced release of retinol from retinol-binding protein. FEBS Lett. 1993 Feb 15;317(3):181-4. Review. PubMed
Reva BA, Finkelstein AV.
A new approach to the design of a sequence with the highest affinity for a molecular surface. Protein Eng. 1992 Oct;5(7):625-8. PubMed
Uverskii VN, Semisotnov GV, Ptitsyn OB.
Molten globule unfolding by strong denaturing agents occurs by the "all or nothing" principle. Biofizika. 1993 Jan-Feb;38(1):37-46. Russian. PubMed
1992
Bychkova VE, Berni R, Rossi GL, Kutyshenko VP, Ptitsyn OB.
Retinol-binding protein is in the molten globule state at low pH. Biochemistry. 1992 Aug 25;31(33):7566-71. PubMed
Dolgikh DA, Kirpichnikov MP, Ptitsyn OB, Fedorov AN, Finkel'shtein AV, Chemeris VV.
De novo proteins with a given spatial structure: new approaches to design and analysis. Mol Biol (Mosk). 1992 Nov-Dec;26(6):1242-50. Russian. PubMed
Fedorov AN, Dolgikh DA, Chemeris VV, Chernov BK, Finkelstein AV, Schulga AA, Alakhov YuB, Kirpichnikov MP, Ptitsyn OB.
De novo design, synthesis and study of albebetin, a polypeptide with a predetermined three-dimensional structure. Probing the structure at the nanogram level. J Mol Biol. 1992 Jun 20;225(4):927-31. PubMed
Finkelstein AV, Reva BA.
Search for the stable state of a short chain in a molecular field. Protein Eng. 1992 Oct;5(7):617-24. PubMed
Sander C, Vriend G, Bazan F, Horovitz A, Nakamura H, Ribas L, Finkelstein AV, Lockhart A, Merkl R, Perry LJ, et al.
Protein design on computers. Five new proteins: Shpilka, Grendel, Fingerclasp, Leather, and Aida. Proteins. 1992 Feb;12(2):105-10. PubMed
Uversky VN, Semisotnov GV, Pain RH, Ptitsyn OB.
'All-or-none' mechanism of the molten globule unfolding. FEBS Lett. 1992 Dec 7;314(1):89-92. PubMed
1991
Damaschun G, Damaschun H, Gast K, Zirwer D, Bychkova VE.
Solvent dependence of dimensions of unfolded protein chains. Int J Biol Macromol. 1991 Aug;13(4):217-21. PubMed
Dolgikh DA, Fedorov AN, Chermeris VV, Chernov BK, Finkel'shtein AV, Shul'ga AA, Alakhov IuB, Kirpichnikov MP, Ptitsyn OB.
Preparation and study of albebetin, an artificial protein with a given spatial structure. Dokl Akad Nauk SSSR. 1991;320(5):1266-9. Russian. PubMed
Finkelstein AV, Badretdinov AY, Ptitsyn OB.
Physical reasons for secondary structure stability: alpha-helices in short peptides. Proteins. 1991;10(4):287-99. PubMed
Finkelstein AV, Reva BA.
A search for the most stable folds of protein chains. Nature. 1991 Jun 6;351(6326):497-9. PubMed
Finkelstein AV.
Rate of beta-structure formation in polypeptides. Proteins. 1991;9(1):23-7. PubMed
Ptitsyn OB.
How does protein synthesis give rise to the 3D-structure? FEBS Lett. 1991 Jul 22;285(2):176-81. Review. PubMed
Semisotnov GV, Rodionova NA, Razgulyaev OI, Uversky VN, Gripas' AF, Gilmanshin RI.
Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers. 1991 Jan;31(1):119-28. PubMed
Semisotnov GV, Vas M, Chemeris VV, Kashparova NJ, Kotova NV, Razgulyaev OI, Sinev MA.
Refolding kinetics of pig muscle and yeast 3-phosphoglycerate kinases and of their proteolytic fragments. Eur J Biochem. 1991 Dec 18;202(3):1083-9. PubMed
1990
Bychkova VE, Bartoshevich SF, Klenin SI.
Comparative study of diffusion coefficients of alpha-lactalbumins and lysozyme using polarization interferometer. Biofizika. 1990 Mar-Apr;35(2):242-8. Russian. PubMed
Chothia C, Finkelstein AV.
The classification and origins of protein folding patterns. Annu Rev Biochem. 1990;59:1007-39. Review. PubMed
Goldberg ME, Semisotnov GV, Friguet B, Kuwajima K, Ptitsyn OB, Sugai S.
An early immunoreactive folding intermediate of the tryptophan synthease beta 2 subunit is a 'molten globule'. FEBS Lett. 1990 Apr 9;263(1):51-6. PubMed
Ptitsyn OB, Pain RH, Semisotnov GV, Zerovnik E, Razgulyaev OI.
Evidence for a molten globule state as a general intermediate in protein folding. FEBS Lett. 1990 Mar 12;262(1):20-4. PubMed
Semisotnov GV, Uversky VN, Sokolovsky IV, Gutin AM, Razgulyaev OI, Rodionova NA.
Two slow stages in refolding of bovine carbonic anhydrase B are due to proline isomerization. J Mol Biol. 1990 Jun 5;213(3):561-8. PubMed
Vas M, Sinev MA, Kotova NV, Semisotnov GV.
Reactivation of 3-phosphoglycerate kinase from its unfolded proteolytic fragments. Eur J Biochem. 1990 May 20;189(3):575-9. PubMed
1989
Crane-Robinson C, Ptitsyn OB.
Binding of the globular domain of linker histones H5/H1 to the nucleosome: a hypothesis. Protein Eng. 1989 Aug;2(8):577-82. Review. PubMed
Finkelstein AV, Janin J.
The price of lost freedom: entropy of bimolecular complex formation. Protein Eng. 1989 Oct;3(1):1-3. PubMed
Finkelstein AV, Shakhnovich EI.
Theory of cooperative transitions in protein molecules. II. Phase diagram for a protein molecule in solution. Biopolymers. 1989 Oct;28(10):1681-94. PubMed
Ptitsyn OB, Finkelstein AV.
Prediction of protein secondary structure based on physical theory. Histones. Protein Eng. 1989 Mar;2(6):443-7. PubMed
Rodionova NA, Semisotnov GV, Kutyshenko VP, Uverskii VN, Bolotina IA.
Staged equilibrium of carbonic anhydrase unfolding in strong denaturants. Mol Biol (Mosk). 1989 May-Jun;23(3):683-92. Russian. PubMed
Semisotnov GV, Kutyshenko VP, Ptitsyn OB.
Intramolecular mobility of a protein in a "molten globule" state. A study of carbonic anhydrase by 1H-NMR. Mol Biol (Mosk). 1989 May-Jun;23(3):808-15. Russian. PubMed
Shakhnovich EI, Finkelstein AV.
Theory of cooperative transitions in protein molecules. I. Why denaturation of globular protein is a first-order phase transition. Biopolymers. 1989 Oct;28(10):1667-80. PubMed
Sinev MA, Razgulyaev OI, Vas M, Timchenko AA, Ptitsyn OB.
Correlation between enzyme activity and hinge-bending domain displacement in 3-phosphoglycerate kinase. Eur J Biochem. 1989 Mar 1;180(1):61-6. PubMed
1988
Bychkova VE, Pain RH, Ptitsyn OB.
The 'molten globule' state is involved in the translocation of proteins across membranes? FEBS Lett. 1988 Oct 10;238(2):231-4. PubMed
Gil'manshin RI, Ptitsyn OB, Semisotnov GV.
Kinetics of the renaturation of bovine alpha-lactalbumin. Biofizika. 1988 Mar-Apr;33(2):204-7. Russian. PubMed
Murzin AG, Finkelstein AV.
General architecture of the alpha-helical globule. J Mol Biol. 1988 Dec 5;204(3):749-69. PubMed
1987
Finkelstein AV, Ptitsyn OB.
Why do globular proteins fit the limited set of folding patterns? Prog Biophys Mol Biol. 1987;50(3):171-90. Review. PubMed
Gilmanshin RI, Ptitsyn OB.
An early intermediate of refolding alpha-lactalbumin forms within 20 ms. FEBS Lett. 1987 Nov 2;223(2):327-9. PubMed
Mesyanzhinov VV, Peletskaya EN, Zhdanov VM, Efimov AV, Finkelstein AV, Ivanovsky DI.
Prediction of secondary structure, spatial organization and distribution of antigenic determinants for hepatitis A virus proteins. J Biomol Struct Dyn. 1987 Oct;5(2):447-58. PubMed
Semisotnov GV, Rodionova NA, Kutyshenko VP, Ebert B, Blanck J, Ptitsyn OB.
Sequential mechanism of refolding of carbonic anhydrase B. FEBS Lett. 1987 Nov 16;224(1):9-13. PubMed
1986
Dolgikh DA, Abaturov LV, Bolotina IA, Brazhnikov EV, Bychkova VE, Gilmanshin RI, Lebedev YuO, Semisotnov GV, Tiktopulo EI, Ptitsyn OB, et al.
Compact state of a protein molecule with pronounced small-scale mobility: bovine alpha-lactalbumin. Eur Biophys J. 1985;13(2):109-21. Erratum in: Eur Biophys J 1986;13(6):381. PubMed
Pavlov MYu, Sinev MA, Timchenko AA, Ptitsyn OB.
A study of apo- and holo-forms of horse liver alcohol dehydrogenase in solution by diffuse x-ray scattering. Biopolymers. 1986 Aug;25(8):1385-97. PubMed
Pfeil W, Bychkova VE, Ptitsyn OB.
Physical nature of the phase transition in globular proteins. Calorimetric study of human alpha-lactalbumin. FEBS Lett. 1986 Mar 31;198(2):287-91. PubMed
Ptitsyn OB, Finkel'shtein AV, Murzin AG.
Predicting the three-dimensional structure of alpha- and beta-interferons. Mol Biol (Mosk). 1986 Jan-Feb;20(1):21-8. Russian. PubMed
Ptitsyn OB, Volkenstein MV.
Protein structure and neutral theory of evolution. J Biomol Struct Dyn. 1986 Aug;4(1):137-56. PubMed
1985
Brazhnikov EV, Chirgadze YuN, Dolgikh DA, Ptitsyn OB.
Noncooperative temperature melting of a globular protein without specific tertiary structure: acid form of bovine carbonic anhydrase B. Biopolymers. 1985 Oct;24(10):1899-907. PubMed
Ptitsyn OB, Finkelstein AV, Murzin AG.
Structural model for interferons. FEBS Lett. 1985 Jul 8;186(2):143-8. PubMed
1984
Dolgikh DA, Kolomiets AP, Bolotina IA, Ptitsyn OB.
'Molten-globule' state accumulates in carbonic anhydrase folding. FEBS Lett. 1984 Jan 2;165(1):88-92. PubMed
Ptitsyn OB.
Protein as an edited random copolymer. Mol Biol (Mosk). 1984 May-Jun;18(3):574-90. Russian. PubMed
1983
Finkelstein AV, Bendzko P, Rapoport TA.
Recognition of signal sequences. FEBS Lett. 1983 Sep 19;161(2):176-9. PubMed
Ptitsyn OB, Dolgikh DA, Gil'manshin RI, Shakhnovich EI, Finkel'shtein AV.
Fluctuating state of the protein globule. Mol Biol (Mosk). 1983 May-Jun;17(3):569-76. Russian. PubMed
Ptitsyn OB, Finkelstein AV.
Theory of protein secondary structure and algorithm of its prediction. Biopolymers. 1983 Jan;22(1):15-25. PubMed
1982
Gil'manshin RI, Dolgikh DA, Ptitsyn OB, Finkel'shtein AV, Shakhnovich EI.
Protein globule without the unique three-dimensional structure: experimental data for alpha-lactalbumins and general model. Biofizika. 1982 Nov-Dec;27(6):1005-16. Russian. PubMed
Ptitsyn OB, Finkelstein AV, Kirpichnikov MP, Skryabin KG.
cI and lexA repressors consist of three cro-like domains. FEBS Lett. 1982 Oct 4;147(1):11-5. PubMed
1981
Bolotina IA, Chekhov VO, Lugauskas VIu, Ptitsyn OB.
Determination of protein secondary structure from circular dichroism spectra. III. Protein-derived base spectra of circular dichroism for antiparallel and parallel beta-structures. Mol Biol (Mosk). 1981 Jan-Feb;15(1):167-75. Russian. PubMed
Dolgikh DA, Gilmanshin RI, Brazhnikov EV, Bychkova VE, Semisotnov GV, Venyaminov SYu, Ptitsyn OB.
Alpha-Lactalbumin: compact state with fluctuating tertiary structure? FEBS Lett. 1981 Dec 28;136(2):311-5. PubMed
Kashparov IA, Semisotnov GV, Alakhov IuB.
Properties and role of tryptophan residues in the polypeptide chain of elongation factor G from E. coli. Biokhimiia. 1981 Aug;46(8):1488-98. Russian. PubMed
Kashparov IA, Semisotnov GV, Alakhov YB.
Interaction of the N-terminal and C-terminal domains of elongation factor G on formation of complexes with guanyl nucleotides. Eur J Biochem. 1981 Aug;118(2):417-21. PubMed
1980
Bolotina IA, Chekhov VO, Lugauskas VIu, Finkel'shtein AV, Ptitsyn OB.
Determination of the secondary structure of proteins from their circular dichroism spectra. I. Protein reference spectra for alpha-, beta- and irregular structures. Mol Biol (Mosk). 1980 Jul-Aug;14(4):891-902. Russian. PubMed
Bolotina IA, Chekhov VO, Lugauskas VIu, Ptitsyn OB.
Determination of the secondary structure of proteins from their circular dichroism spectra. II. Estimation of the contribution of beta-pleated sheets. Mol Biol (Mosk). 1980 Jul-Aug;14(4):902-9. Russian. PubMed
Bychkova VE, Semisotnov GV, Ptitsyn OB, Gudkova OV, Mitin IuV.
Compact structure of random copolymers of hydrophobic and hydrophilic amino acid residues. Mol Biol (Mosk). 1980 Mar-Apr;14(2):278-86. Russian. PubMed
Ptitsyn OB, Finkelstein AV.
Similarities of protein topologies: evolutionary divergence, functional convergence or principles of folding? Q Rev Biophys. 1980 Aug;13(3):339-86. Review. PubMed
1979
Finkel'shtein AV, Ptitsyn OB, Bendzko P.
Folding and topology of antiparallel beta-structure. Biofizika. 1979 Jan-Feb;24(1):21-6. Russian. PubMed
Ptitsyn OB, Finkel'shtein AV.
Folding and topology of parallel beta-structure. Biofizika. 1979 Jan-Feb;24(1):27-31. Russian. PubMed
Ptitsyn OB, Finkelstein AV, Falk P.
Principal folding pathway and topology of all-beta proteins. FEBS Lett. 1979 May 1;101(1):1-5. PubMed
1978
Finkel'shtein AV, Ptitsyn OB.
Theory of self-organization of the secondary structure of proteins: relationship between native globule structure and the secondary structure of the unfolded chain. Dokl Akad Nauk SSSR. 1978;242(5):1226-8. Russian. PubMed
Ptitsyn OB.
Inter-domain mobility in proteins and its probable functional role. FEBS Lett. 1978 Sep 1;93(1):1-4. PubMed
Timchenko AA, Ptitsyn OB, Dolgikh DA, Fedorov BA.
The structure of ribonuclease in solution does not differ from its crystalline structure. FEBS Lett. 1978 Apr 1;88(1):105-8. PubMed
Timchenko AA, Ptitsyn OB, Troitsky AV, Denesyuk AI.
The structure of phage T4 lysozyme in solution noticeably differs from its crystalline struction. FEBS Lett. 1978 Apr 1;88(1):109-13. PubMed
1977
Fedorov BA, Ptitsyn OB.
Nature of the 4.5 Angstrom-maximum in x-ray diffraction curves of proteins and structured polypeptides. Dokl Akad Nauk SSSR. 1977 Apr 1;233(4):716-8. Russian. PubMed
Finkelstein AV, Ptitsyn OB, Kozitsyn SA.
Theory of protein molecule self-organization. II. A comparison of calculated thermodynamic parameters of local secondary structures with experiments. Biopolymers. 1977 Mar;16(3):497-524. PubMed
Finkelstein AV, Ptitsyn OB.
Theory of protein molecule self-organization. I. Thermodynamic parameters of local secondary structures in the unfolded protein chain. Biopolymers. 1977 Mar;16(3):469-95. PubMed
Finkelstein AV.
Did the primitive ribosomal RNA code primitive ribosomal protein? FEBS Lett. 1977 Oct 15;82(2):169-71. PubMed
Finkelstein AV.
Theory of protein molecule self-organization. III. A calculating method for the probabilities of the secondary structure formation in an unfolded polypeptide chain. Biopolymers. 1977 Mar;16(3):525-9. PubMed
1976
Bychkova VE, Ptitsyn OB.
Thermodynamic parameters of helix-random coil transitions in polypeptide chains. IV. Random copolymers of L-alanine with L-glutamic acid. Mol Biol (Mosk). 1976 Jul-Aug;10(4):756-61. PubMed
Finkelstein AV, Ptitsyn OB.
A theory of protein molecule self-organization. IV. Helical and irregular local structures of unfolded protein chains. J Mol Biol. 1976 May 5;103(1):15-24. PubMed
Timchenko AA, Ptitsyn OB, Serdiuk IN, Fedorov BA, Kravchenko NA.
Structure of lysozyme and its complex with an inhibitor in solution: comparison with crystalline structures. Dokl Akad Nauk SSSR. 1976 Sep 11;230(2):458-61. Russian. PubMed
1975
Anufrieva EV, Bychkova VE, Krakovyak MG, Pautov VD, Ptitsyn OB.
A synthetic polypeptide with a compact structure and its self-organization. FEBS Lett. 1975 Jul 15;55(1):46-9. PubMed
Bychkova VE, Gudkov AT, Miller WG, Mitin YV, Ptitsyn OB, Shpungin IL.
Thermodynamic parameters of the helix-coil transition in polypeptide chains. III. Random copolymers of L-leucine and L-glutamic acid. Biopolymers. 1975 Aug;14(8):1739-53. PubMed
Finkelstein AV, Kozitsyn SA, Ptitsyn OB.
Prediction of the three-dimensional structure for ribosomal protein L25. FEBS Lett. 1975 Dec 1;60(1):137-40. PubMed
Kozitsyn SA, Ptitsyn OB.
The structure of hydrophobic cores of globins. Mol Biol. 1975 Jan;8(4):427-33. PubMed
Ptitsyn OB, Rashin AA.
A model of myoglobin self-organization. Biophys Chem. 1975 Feb;3(1):1-20. PubMed
Ptitsyn OB.
Multicenter mechanism of self-organization of globular proteins and cooperativity of their denaturation and renaturation. Dokl Akad Nauk SSSR. 1975 Aug 11;223(5):1253-5. Russian. PubMed
1974
Denesiuk AI, Ptitsyn OB, Finkel'shtein AV.
Letter: Helical structure of unfolded protein chains. Biofizika. 1974 May-Jun;19(3):549-61. Russian. PubMed
Fedorov BA, Voronin LA, Ptitsyn OB.
X-ray diffuse scattering by polypeptides and proteins in solution. IV. Consideration of the solvent effect for globular protein solutions. Mol Biol. 1974 Sep-Oct;8(5):693-702. Russian. PubMed
Grigor'ev AI, Volkova LA, Ptitsyn OB.
Diffuse scattering of x-rays by solutions of synthetic polypeptides and globular proteins. Mol Biol. 1974 Mar;7(5):541-8. PubMed
Schulz GE, Barry CD, Friedman J, Chou PY, Fasman GD, Finkelstein AV, Lim VI, Pititsyn OB, Kabat EA, Wu TT, Levitt M, Robson B, Nagano K.
Comparison of predicted and experimentally determined secondary structure of adenyl kinase. Nature. 1974 Jul 12;250(462):140-2. PubMed
1973
Bychkova VE.
Nurses' functions in the stomatological department. Med Sestra. 1973 Mar;32(3):27. Russian. PubMed
Ptitsyn OB, Denesyuk AI, Finkelstein AV, Lim VI.
Prediction of the secondary structure of the L7, L12 proteins of the E. coli ribosome. FEBS Lett. 1973 Aug 1;34(1):55-7. PubMed
Ptitsyn OB, Rashin AA.
Self-organization of the myoglobin molecule. Dokl Akad Nauk SSSR. 1973 Nov 11;213(2):473-5. Russian. PubMed
Ptitsyn OB.
Stages in the mechanism of self-organization of protein molecules. Dokl Akad Nauk SSSR. 1973 Jun 11;210(5):1213-5. Russian. PubMed
1972
Fedorov BA, Ptitsyn OB, Voronin LA.
X-Ray diffuse scattering of globular protein solutions: Consideration of the solvent influence. FEBS Lett. 1972 Dec 1;28(2):188-190. PubMed
Lim VI, Ptitsyn OB.
Lattice model of portions of the protein molecule hydrophobic nucleus. Biofizika. 1972 Jan-Feb;17(1):21-33. Russian. PubMed
Ptitsyn OB.
Thermodynamic parameters of helix-coil transitions in polypeptide chains. Pure Appl Chem. 1972;31(1):227-44. PubMed
1971
Barskaya TV, Ptitsyn OB.
Thermodynamic parameters of helix-coil transition in polypeptide chains. II. Poly-L-lysine. Biopolymers. 1971 Nov;10(11):2181-97. PubMed
Bychkova VE, Ptitsyn OB, Barskaya TV.
Thermodynamic parameters of helix-coil transition in polypeptide chains. I. Poly-(L-glutamic acid). Biopolymers. 1971 Nov;10(11):2161-79. PubMed
Finkelstein AV, Ptitsyn OB.
Statistical analysis of the correlation among amino acid residues in helical, beta-structural and non-regular regions of globular proteins. J Mol Biol. 1971 Dec 28;62(3):613-24. PubMed
Grigor'ev AI, Volkova LA, Ptitsyn OB.
Identification of alpha-spiral structure of polypeptide chains in solution by x-ray diffusion scattering. Dokl Akad Nauk SSSR. 1971 Jan 21;196(3):711-2. Russian. PubMed
Grigoryev AI, Volkova LA, Ptitsyn OB.
Effect of the secondary structure of globular proteins in solution on the indicatrix of x-ray diffusion scattering.FEBS Lett. 1971 Jun 24;15(3):217-219. PubMed
Grigoryev AI, Volkova LA, Ptitsyn OB.
Identification of the secondary structure of polypeptide chains in solution by x-ray diffusion scattering. FEBS Lett. 1971 Apr 30;14(3):189-191. PubMed
1970
Ptitsyn OB, Finkel'shtein AV.
Predicting the spiral portions of globular proteins from their primary structure. Dokl Akad Nauk SSSR. 1970;195(1):221-4. Russian. PubMed
Ptitsyn OB, Finkel'shtein AV.
Relation of the secondary structure of globular proteins to their primary structure. Biofizika. 1970 Sep-Oct;15(5):757-68. Russian. PubMed
Ptitsyn OB.
The physical principles of the self-organization of protein bonds. Usp Sovrem Biol. 1970 Jan-Feb;69(1):26-48. Review. Russian. PubMed
Serdyuk IN, Smirnov NI, Ptitsyn OB, Fedorov BA.
On the presence of a dense internal region in the 50 S subparticle of E. coli ribosomes. FEBS Lett. 1970 Sep 7;9(6):324-326. PubMed
1969
Ptitsyn OB.
Statistical analysis of the distribution of amino acid residues among helical and non-helical regions in globular proteins. J Mol Biol. 1969 Jun 28;42(3):501-10. PubMed
1967
Birshtein TM, Ptitsyn OB.
Dipole-dipole interaction and the beta structure of synthetic polypeptides. Biopolymers. 1967;5(8):785-7. PubMed
El'iashevich AM, Ptitsyn OB.
Effect of electrostatic interactions on the dimensions of native DNA molecules. Biofizika. 1967 Jul-Aug;12(4):581-5. Russian. PubMed
Ptitsyn OB, Barskaya TV, Bolotina IA, Illarionova IG.
Synthetic polypeptides. 3. Comparison of the degree of cooperation of the helical state of poly-L-glutaminic acid in various solvents. Biofizika. 1967 May-Jun;12(3):386-96. Russian. PubMed
Ptitsyn OB.
The nature of forces determining the inherent spatial structure of globular proteins. Usp Sovrem Biol. 1967 Jan-Feb;63(1):3-27. Review. Russian. PubMed
1966
Anufrieva EV, Bolotina IA, Volchek BZ, Illarionova NG, Kalikhevich VI, Korotkina OZ, Mitin YV, Ptitsyn OB, Purkina AV, Eskin VE.
Investigations of synthetic polypeptides: transitions-intramolecular beta-structures-coil in poly-S-carbobenzoxymethyl-L-cysteine. Fed Proc Transl Suppl. 1966 Nov-Dec;25(6):1045-50. PubMed
Illarionova NG, Bolotina IA, Volchek BZ, Kalikhevich VI, Mitin IuV, Ptitsyn OB, Purkina AV.
Studies of synethtic polypeptides. II. Beta-structure--coil transition of poly-S-carboxymethyl-L-cysteine under changes of medium pH and temperature. Biofizika. 1966;11(5):762-5. Russian. PubMed
Ptitsyn OB, Skvortsov AM.
Hydrophobic interactions and nucleoprotein structure. Biofizika. 1966;11(1):3-6. Russian. PubMed
1965
Anufrieva EV, Bolotina IA, Volchek BZ, Illarionova NG, Kalikhevich VI, Korotkina OZ, Mitin IuV, Ptitsyn OB, Purkina AV, Eskin VE.
Study of synthetic polypeptides. I. Transformations-intramolecular beta-structure coil in poly-S-carbobenzoxymethyl-L-cysteine. Biofizika. 1965;10(6):918-28. Russian. PubMed
Anufrieva EV, Volchek BZ, Illarionova NG, Kalikhevich VN, Korotkina OZ, Mitin IuV, Ptitsyn OB, Purkina AV, Eskin VE.
Synthesis of poly-S-carbobenzomethoxy-L-cysteine and studies on its structure. Biofizika. 1965;10(2):346-7. Russian. PubMed
Ptitsyn OB, Eizner IuE.
The theory of helix-coil transitions in macromolecules. Biofizika. 1965;10:3-6. Russian. PubMed
Ptitsyn OB, Skvortsov AM.
Theory of helix-coil transformation in biopolymers. V. A method of determining cooperativeness of helix-coil transformation in polypeptide chains by changing molecule size in the transformation region. Biofizika. 1965;10(6):909-17. Russian. PubMed
1963
Ptitsyn OB, Fedorov BA.
Determination of flexibility of DNA molecules with the aid of light disseminated at large angles. Biofizika. 1963;78:659-63. Russian. PubMed
Ptitsyn OB, Fedorov BA.
On a study of the structure of molecules of native RNA by the method of scattering roentgen rays at small angels. Tsitologiia. 1963 May-Jun;18:352-3. Russian. PubMed
Vol'kenshtein MV, Godzhaev NM, Gotlib IuA, Ptitsyn OB.
On the kinetics of biosynthesis. Biofizika. 1963;8:3-8. Russian. PubMed
1962
Ptitsyn OB.
The theory of spiral-coil transition in biopolymers. II. The role of distant order interaction in DNA denaturation. Biofizika. 1962;7:257-62. Russian. PubMed
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