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- Mirrored Resources:
- Protein Data Bank - PDB, ftp mirror
- Structural Classification of Proteins - SCOP
- Prediction of protein structure by Burkhard Rost
- BLAST - mirror
- Some mirrored NCBI databases, ftp
- Resources Developed in Our Laboratory:
- Lectures of A.V.Finkelstein on Protein Physics:
- Lectures on Structures and Functions of Proteins. Moscow State University, 2014 (in Russian)
- Финкельштейн А.В., Птицын О.Б. Физика белка: курс лекций. 3-е изд., испр. и доп. - М.:КДУ, 2012. PDF
- Lectures of A.V.Finkelstein on Protein Physics, 1999-2000 (in Russian)
- Slides for Lectures of A.V.Finkelstein on Protein Physics
- Tasks for Lectures of A.V.Finkelstein on Protein Physics
- Miscellaneous resources:
- A1 – ENCAD: interactions
(In English: PDF, DOC. In Russian: PDF, DOC)
- A2 – Database for molecular crystals (PDF)
- Additions and corrections to supplement A2 (PDF, DOC)
- Programs:
- Prediction of Secondary Protein Structure - ALB
- Programs for Threading in a Sequence Consistent Field:
- SeqCF_1_THREADER
- THREADER 02
- Program for Prediction of Disordered Regions in Proteins - FoldUnfold
- Galzitskaya O.V., Garbuzynskiy S.O., Lobanov M.Yu. (2006). FoldUnfold: web server for the prediction of disordered regions in protein chain. Bioinformatics, v.22 (23), pp. 2948-2949.
- Prediction of protein domain boundaries from sequence alone.
- Galzitskaya O.V., Melnik B.S. (2003). Prediction of protein domain boundaries from sequence alone. Protein Science, v.12, pp. 696-701.
- Prediction of number and position of domain boundaries in multi-domain proteins.
- Galzitskaya O.V., Dovidchenko N.V., Lobanov M.Yu., Garbuzynskiy S.O. (2006). Prediction of protein domain boundaries from statistics of appearance of amino acid residues. Molecular Biology, v.40 (1), pp. 96-106.
- Databases :
- Database of structural pairs of proteins from thermo- and mesophilic organisms
- Experimentally measured and theoretically predicted phi-values.
- Garbuzynskiy S.O., Finkelstein A.V., Galzitskaya O.V. (2005). On the prediction of folding nuclei in globular proteins. Molecular Biology, v.39 (6), pp. 906-914.
- Database of X-Ray and NMR 3D structures of the same proteins.
- Garbuzynskiy S.O., Melnik B.S., Lobanov M.Yu., Finkelstein A.V., Galzitskaya O.V. (2005). Comparison of X-ray and NMR structures: is there a systematic difference in residue contacts between X-ray- and NMR-resolved protein structures? Proteins: Structure, Function, and Bioinformatics, v.60 (1), pp. 139-147.
- Database of 3D structures of "ideally" folded proteins.
- Garbuzynskiy S.O., Lobanov M.Yu., Galzitskaya O.V. (2004). To be folded or to be unfolded? Protein Science, v.13 (11), pp. 2871-2877.
- Database of 3D structures with identity below 80%.
- Galzitskaya O.V., Garbuzynskiy S.O., Lobanov M.Yu. (2006). Prediction of natively unfolded regions in protein chains. Molecular Biology, v.40 (2), pp. 298-304.
- Database of natively unfolded proteins.
- Galzitskaya O.V., Garbuzynskiy S.O., Lobanov M.Yu. (2006). Prediction of natively unfolded regions in protein chains. Molecular Biology, v.40 (2), pp. 298-304.
- Database of 559 globular proteins.
- Galzitskaya O.V., Garbuzynskiy S.O., Lobanov M.Yu. (2006). Prediction of natively unfolded regions in protein chains. Molecular Biology, v.40 (2), pp. 298-304.
- Database of 80 globular proteins.
- Galzitskaya O.V., Garbuzynskiy S.O., Lobanov M.Yu. (2006). Prediction of natively unfolded regions in protein chains. Molecular Biology, v.40 (2), pp. 298-304.
- Useful Links
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