A. V. Finkelstein

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Physical reasons for secondary structure stability: α‐Helices in short peptides

O. Ptitsyn, A. V. Finkelstein, A. Y. Badretdinov, 1991 .

Theory of protein secondary structure and algorithm of its prediction

A. Finkelstein, O. Ptitsyn, A. V. Finkelstein, 1983, Biopolymers.

Why do globular proteins fit the limited set of folding patterns?

O. Ptitsyn, A. V. Finkelstein, 1987, Progress in biophysics and molecular biology.

Theory of cooperative transitions in protein molecules. I. Why denaturation of globular protein is a first‐order phase transition

E I Shakhnovich, E. Shakhnovich, A. V. Finkelstein, 1989, Biopolymers.

O. Ptitsyn, A. V. Finkelstein, 1980, Quarterly Reviews of Biophysics.

Structural model for interferons

A G Murzin, O. Ptitsyn, A. Murzin, 1985, FEBS letters.

General architecture of the α-helical globule

Alexey G. Murzin, A. Murzin, A. V. Finkelstein, 1988 .

Statistical analysis of the correlation among amino acid residues in helical, beta-structural and non-regular regions of globular proteins.

O. Ptitsyn, A. V. Finkelstein, A V Finkelstein, 1971, Journal of molecular biology.

Folding Nuclei in Proteins

O. V. Galzitskaya, A. V. Finkelstein, O. Galzitskaya, 2001, Molecular Biology.

cI and lexA repressors consist of three cro‐like domains

O. Ptitsyn, A. V. Finkelstein, M. P. Kirpichnikov, 1982, FEBS letters.

How to determine the size of folding nuclei of protofibrils from the concentration dependence of the rate and lag-time of aggregation. II. Experimental application for insulin and LysPro insulin: aggregation morphology, kinetics, and sizes of nuclei.

A. V. Finkelstein, N. Dovidchenko, O. Galzitskaya, 2014, The journal of physical chemistry. B.

PHYSICAL REASON FOR FAST FOLDING OF THE STABLE SPATIAL STRUCTURE OF PROTEINS : A SOLUTION OF THE LEVINTHAL PARADOX

A. Badretdinov, A. V. Finkelstein, 1997 .

Prediction of the secondary structure of the L7, L12 proteins of the E. coli ribosome

V. Lim, O. Ptitsyn, A. V. Finkelstein, 1973, FEBS letters.

Cunning simplicity of a stoichiometry driven protein folding thesis.

A. V. Finkelstein, O. Galzitskaya, M. Y. Lobanov, 2011, Journal of biomolecular structure & dynamics.

Protein Biosynthesis Proofreading Is Closely Associated with the Existence of Factor-Free Ribosomal Synthesis

A. V. Finkelstein, L. P. Gavrilova, 2019, Molecular Biology.

Physical Basis of Functioning of Antifreeze Protein

A. V. Finkelstein, B. S. Melnik, 2022, Molecular Biology.

Atomic force field FFsol for calculating molecular interactions in water environment

A. V. Finkelstein, L. Pereyaslavets, Alexei V. Finkelstein, 2010, Molecular Biology.

MECHANISM OF SELF-ORGANIZATION OF THE TERTIARY STRUCTURE OF GLOBULAR PROTEINS

O. Ptitsyn, A. V. Finkelstein, 1981 .

Development and testing of PFFSol1.1, a new polarizable atomic force field for calculation of molecular interactions in implicit water environment.

A. V. Finkelstein, L. Pereyaslavets, 2012, The journal of physical chemistry. B.

Theory of cooperative transitions in protein molecules. II. Phase diagram for a protein molecule in solution

A. V. Finkelstein, E. Shakhnovich, 1989, Biopolymers.

Theory of protein molecule self‐organization. I. Thermodynamic parameters of local secondary structures in the unfolded protein chain

A. Finkelstein, O. Ptitsyn, A. V. Finkelstein, 1977, Biopolymers.

Comparison of predicted and experimentally determined secondary structure of adenyl kinase

C. D. Barry, T. T. Wu, M. Levitt, 1974, Nature.

How to determine the size of folding nuclei of protofibrils from the concentration dependence of the rate and lag-time of aggregation. I. Modeling the amyloid protofibril formation.

A. V. Finkelstein, N. Dovidchenko, O. Galzitskaya, 2014, The journal of physical chemistry. B.

Theory of protein molecule self‐organization. II. A comparison of calculated thermodynamic parameters of local secondary structures with experiments

A. Finkelstein, O. Ptitsyn, A. V. Finkelstein, 1977, Biopolymers.

Principal folding pathway and topology of all‐β proteins

O. Ptitsyn, A. V. Finkelstein, P. Falk, 1979 .

Folding of circular permutants with decreased contact order: general trend balanced by protein stability.

A. Finkelstein, A. V. Finkelstein, D. Otzen, 2001, Journal of molecular biology.

Determination of the Size of the Primary and Secondary Folding Nuclei of Protofibrils from the Concentration Dependence of the Rate and the Lag-Time of Their Formation

A. V. Finkelstein, N. Dovidchenko, O. Galzitskaya, 2015 .

Accurate general method for lattice approximation of three‐dimensional structure of a chain molecule

A V Finkelstein, B A Reva, A. V. Finkelstein, 1995, Proteins.

Did the primitive ribosomal RNA code primitive ribosomal protein?

A. V. Finkelstein, 1977, FEBS letters.

Inclusion of the most important multi-particle interactions in the amber force field and application of the revised force field to molecular dynamics calculations

A. V. Finkelstein, O. Galzitskaya, A. Glyakina, 2015 .

Mechanism of protein folding

O. Ptitsyn, A. V. Finkelstein, 1979 .

A theory of protein molecule self-organization. IV. Helical and irregular local structures of unfolded protein chains.

O. Ptitsyn, A. V. Finkelstein, A V Finkelstein, 1976, Journal of molecular biology.

Short alpha-helix stability

O. Ptitsyn, A. V. Finkelstein, A. Y. Badretdinov, 1990, Nature.