Підписатись
Alexei Finkelstein
Alexei Finkelstein
Институт белка РАН
Підтверджена електронна адреса в vega.protres.ru
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Посилання
Посилання
Рік
Making optimal use of empirical energy functions: force‐field parameterization in crystal space
E Krieger, T Darden, SB Nabuurs, A Finkelstein, G Vriend
Proteins: Structure, Function, and Bioinformatics 57 (4), 678-683, 2004
10182004
Protein physics: a course of lectures (soft condensed matter, complex fluids and biomaterials)
AV Finkelstein, O Ptitsyn
Protein physics: a course of lectures (soft condensed matter, complex fluids …, 2016
689*2016
Contact order revisited: influence of protein size on the folding rate
DN Ivankov, SO Garbuzynskiy, E Alm, KW Plaxco, D Baker, AV Finkelstein
Protein science 12 (9), 2057-2062, 2003
4542003
The classification and origins of protein folding patterns
C Chothia, AV Finkelstein
Annual review of biochemistry 59 (1), 1007-1035, 1990
4361990
The price of lost freedom: entropy of bimolecular complex formation
AV Finkelstein, J Janin
Protein Engineering, Design and Selection 3 (1), 1-3, 1989
4201989
A theoretical search for folding/unfolding nuclei in three-dimensional protein structures
OV Galzitskaya, AV Finkelstein
Proceedings of the National Academy of Sciences 96 (20), 11299-11304, 1999
3841999
Theory of cooperative transitions in protein molecules. I. Why denaturation of globular protein is a first‐order phase transition
EI Shakhnovich, AV Finkelstein
Biopolymers: Original Research on Biomolecules 28 (10), 1667-1680, 1989
3761989
Why do globular proteins fit the limited set of folding patterns?
AV Finkelstein, OB Ptitsyn
Progress in biophysics and molecular biology 50 (3), 171-190, 1987
3531987
Theory of protein secondary structure and algorithm of its prediction
OB Ptitsyn, AV Finkelstein
Biopolymers: Original Research on Biomolecules 22 (1), 15-25, 1983
3241983
What is the probability of a chance prediction of a protein structure with an RMSD of 6 A?
SJ Reva BA, Finkelstein AV
Folding & Design 3, 141-147, 1998
302*1998
Prediction of protein folding rates from the amino acid sequence-predicted secondary structure
DN Ivankov, AV Finkelstein
Proceedings of the National Academy of Sciences 101 (24), 8942-8944, 2004
2542004
Similarities of protein topologies: evolutionary divergence, functional convergence or principles of folding?
OB Ptitsyn, AV Finkelstein
Quarterly Reviews of Biophysics 13 (3), 339-386, 1980
2491980
Why do protein architectures have Boltzmann‐like statistics?
AV Finkelstein, AY Badretdinov, AM Gutin
Proteins: Structure, Function, and Bioinformatics 23 (2), 142-150, 1995
2391995
Rate of protein folding near the point of thermodynamic equilibrium between the coil and the most stable chain fold
AV Finkelstein, AY Badretdinov
Folding and Design 2 (2), 115-121, 1997
2361997
Theory of cooperative transitions in protein molecules. II. Phase diagram for protein molecule in solution , 1989, 28: 1681-1694.
SEI Finkelstein A.V.
Biopolymers 28, 1681-1694, 1989
201*1989
Chain length is the main determinant of the folding rate for proteins with three‐state folding kinetics
OV Galzitskaya, SO Garbuzynskiy, DN Ivankov, AV Finkelstein
Proteins: Structure, Function, and Bioinformatics 51 (2), 162-166, 2003
1872003
A Search for the Most Stable Folds of Protein Chains
RBA Finkelstein AV
Nature 351, 497-499, 1991
1811991
Comparison of predicted and experimentally determined secondary structure of adenyl kinase
NK Schulz G.E., Barry C.D., Friedman J., Chou P.Y., Fasman G.D., Finkelstein ...
Nature 250, 140-142, 1974
1751974
General architecture of the α-helical globule
AG Murzin, AV Finkelstein
Journal of molecular biology 204 (3), 749-769, 1988
1661988
Physics of protein folding
AV Finkelstein, OV Galzitskaya
Physics of Life reviews 1 (1), 23-56, 2004
1502004
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