A. Finkelstein

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Comparison of predicted and experimentally determined secondary structure of adenyl kinase

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

Physical reasons for secondary structure stability: alpha-helices in short peptides.

A. Finkelstein, O. Ptitsyn, A. Badretdinov, 1991, Proteins.

Residue-residue mean-force potentials for protein structure recognition.

A. Finkelstein, B. Reva, M. Sanner, 1997, Protein engineering.

From analysis of protein structural alignments toward a novel approach to align protein sequences

A. Finkelstein, S. Sunyaev, M. Roytberg, 2004, Proteins.

What is the probability of a chance prediction of a protein structure with an rmsd of 6 A?

J. Skolnick, A. Finkelstein, B. Reva, 1998, Folding & design.

Theoretical study of a landscape of protein folding-unfolding pathways. Folding rates at midtransition.

A. Finkelstein, D. Ivankov, 2001, Biochemistry.

A theoretical search for folding/unfolding nuclei in three-dimensional protein structures.

A. Finkelstein, O. Galzitskaya, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Outlining folding nuclei in globular proteins.

A. Finkelstein, O. Galzitskaya, S. O. Garbuzynskiy, 2004, Journal of molecular biology.

Why do protein architectures have boltzmann‐like statistics?

A. Finkelstein, A. Badretdinov, A. Gutin, 1995, Proteins.

Life in Phases: Intra- and Inter- Molecular Phase Transitions in Protein Solutions

A. Finkelstein, V. Uversky, 2019, Biomolecules.

Common features in structures and sequences of sandwich-like proteins

Israel M. Gelfand, Alexei V. Finkelstein, I. Gelfand, 2002, Proceedings of the National Academy of Sciences of the United States of America.

A structural perspective of compensatory evolution

A. Finkelstein, D. Ivankov, F. Kondrashov, 2014, Current opinion in structural biology.

Folding of chains with random and edited sequences: similarities and differences.

A. Finkelstein, O. Galzitskaya, 1995, Protein engineering.

Restrictions to protein folding determined by the protein size

A. Finkelstein, S. O. Garbuzynskiy, N. S. Bogatyreva, 2013, FEBS letters.

Averaging interaction energies over homologs improves protein fold recognition in gapless threading

J. Skolnick, A. Finkelstein, B. Reva, 1999, Proteins.

Contact order revisited: Influence of protein size on the folding rate

Kevin W Plaxco, David Baker, Dmitry N Ivankov, 2003, Protein science : a publication of the Protein Society.

Chain length is the main determinant of the folding rate for proteins with three‐state folding kinetics

Dmitry N Ivankov, Oxana V Galzitskaya, Alexei V Finkelstein, 2003, Proteins.

The classification and origins of protein folding patterns.

A V Finkelstein, C Chothia, C. Chothia, 1990, Annual review of biochemistry.

A search for the most stable folds of protein chains

Alexei V. Finkelstein, Boris A. Reva, A. Finkelstein, 1991, Nature.

Two Views on the Protein Folding Puzzle

A. Finkelstein, O. Galzitskaya, D. Ivankov, 2018 .

50+ Years of Protein Folding

A. Finkelstein, A. V. Finkelstein, 2018, Biochemistry (Moscow).

There and back again: Two views on the protein folding puzzle.

A. Finkelstein, O. Galzitskaya, D. Ivankov, 2017, Physics of life reviews.

Weak points of antiparallel β-sheets. How are they filled up in globular proteins?

Haruki Nakamura, Alexei V. Finkelstein, A. Finkelstein, 1993 .

Prediction of protein folding rates from the amino acid sequence-predicted secondary structure

A. Finkelstein, D. Ivankov, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Protein Structure and Its Folding Rate

A. Finkelstein, O. Galzitskaya, D. Ivankov, 2008 .

Rate of protein folding near the point of thermodynamic equilibrium between the coil and the most stable chain fold.

A V Finkelstein, A. Finkelstein, A. Badretdinov, 1997, Folding & design.

Folding nuclei in proteins

Oxana V. Galzitskaya, Alexei V. Finkelstein, Dmitry N. Ivankov, 2001 .

Golden triangle for folding rates of globular proteins

A. Finkelstein, D. Ivankov, S. O. Garbuzynskiy, 2012, Proceedings of the National Academy of Sciences.

Sublimation Entropy and Dissociation Constants Prediction by Quantitative Evaluation of Molecular Mobility in Crystals.

A. Finkelstein, S. O. Garbuzynskiy, 2017, The journal of physical chemistry letters.

Evaluation of the Accuracy of Calculation of the Standard Binding Entropy of Molecules from their Average Mobility in Molecular Crystals

A. Finkelstein, S. O. Garbuzynskiy, 2018, Molecular Biology.

De novo design, synthesis and study of albebetin, a polypeptide with a predetermined three-dimensional structure. Probing the structure at the nanogram level.

A. Finkelstein, O. Ptitsyn, B. Chernov, 1992, Journal of molecular biology.

Reduction of the Search Space for the Folding of Proteins at the Level of Formation and Assembly of Secondary Structures: A New View on the Solution of Levinthal's Paradox.

A. Finkelstein, S. O. Garbuzynskiy, 2015, Chemphyschem : a European journal of chemical physics and physical chemistry.

Search for the most stable folds of protein chains: III. Improvement in fold recognition by averaging over homologous sequences and 3D structures

M. Y. Lobanov, A. Finkelstein, D. S. Rykunov, 2000 .

Search for the most stable folds of protein chains: III. Improvement in fold recognition by averaging over homologous sequences and 3D structures.

M. Y. Lobanov, A. Finkelstein, D. S. Rykunov, 2000, Proteins.

Frontiers in Protein and Peptide Sciences

Wei Chen, Hui Ding, Kuo-Chen Chou, 2014 .

Rate of beta-structure formation in polypeptides.

A. Finkelstein, 1991, Proteins.

The Molten Globule State of a Globular Protein in a Cell Is More or Less Frequent Case Rather than an Exception

A. Finkelstein, V. Bychkova, D. Dolgikh, 2022, Molecules.

Protein Folding: Enigma and Solution

A. Finkelstein, 2022 .

Protein folding problem: enigma, paradox, solution

A. Finkelstein, D. Ivankov, S. O. Garbuzynskiy, 2022, Biophysical Reviews.

50+ Years of Protein Folding

A. Finkelstein, 2018, Biochemistry (Moscow).

Calculation of mobility and entropy of the binding of molecules by crystals

A. Finkelstein, S. O. Garbuzynskiy, 2016, Molecular Biology.

How Can Ice Emerge at 0 °C?

A. Finkelstein, B. Melnik, S. O. Garbuzynskiy, 2022, Biomolecules.

Does AlphaFold predict the spatial structure of a protein from physics or recognize it (its main parts and their association) using databases?

A. Finkelstein, 2022, bioRxiv.

Threading with chemostructural restrictions method for predicting fold and functionally significant residues: Application to dipeptidylpeptidase IV (DPP‐IV)

Alexei Finkelstein, Sid Topiol, A. Finkelstein, 2002, Proteins.

Making optimal use of empirical energy functions: Force‐field parameterization in crystal space

Gert Vriend, Elmar Krieger, Tom Darden, 2004, Proteins.

Intermediate states of apomyoglobin: Are they parts of the same area of conformations diagram?

A. Finkelstein, V. Bychkova, V. Balobanov, 2017, Biochemistry (Moscow).

The Reverse Side of a Coin: “Factor-Free” Ribosomal Protein Synthesis In Vitro is a Consequence of the In Vivo Proofreading Mechanism

A. Finkelstein, 2019, Biomolecules.

Intersubunit Mobility of the Ribosome

A. Spirin, A. Finkelstein, S. Razin, 2018, Molecular Biology.

Calculation of Crystal-Solution Dissociation Constants

A. Finkelstein, S. O. Garbuzynskiy, 2022, Biomolecules.

3D Protein Folds: Homologs Against Errors-a Simple Estimate Based on the Random Energy Model

Alexei V. Finkelstein, A. Finkelstein, 1998 .

Trend of Amino Acid Composition of Proteins of Different Taxa

Oxana V. Galzitskaya, Alexei V. Finkelstein, Natalya S. Bogatyreva, 2006, J. Bioinform. Comput. Biol..

Why are the same protein folds used to perform different functions?

A. Finkelstein, A. Badretdinov, Alexei V. Finkelstein, 1993, FEBS letters.

Protein structure: what is it possible to predict now?

A V Finkelstein, A. Finkelstein, 1997, Current opinion in structural biology.

Perfect temperature for protein structure prediction and folding

A. Finkelstein, A. Badretdinov, A. Gutin, 1995, Proteins.

Boltzmann-like statistics of protein architectures. Origins and consequences.

A V Finkelstein, A. Finkelstein, A. Gutin, 1995, Sub-cellular biochemistry.

The price of lost freedom: entropy of bimolecular complex formation.

A V Finkelstein, J. Janin, A. Finkelstein, 1989, Protein engineering.

A novel view on the mechanism of biological activity of antifreeze proteins

A. Finkelstein, B. Melnik, I. Balalaeva, 2021, bioRxiv.

Physics of protein folding

Oxana V. Galzitskaya, Alexei V. Finkelstein, A. Finkelstein, 2004 .

The Molten Globule Concept: 45 Years Later

A. Finkelstein, V. Bychkova, G. Semisotnov, 2018, Biochemistry (Moscow).

Solution of Levinthal’s Paradox and a Physical Theory of Protein Folding Times

Dmitry N Ivankov, Alexei V Finkelstein, A. Finkelstein, 2020, Biomolecules.

Some additional remarks to the solution of the protein folding puzzle: Reply to comments on "There and back again: Two views on the protein folding puzzle".

A. Finkelstein, 2017, Physics of life reviews.

Levinthal’s question answered … again?

A. Finkelstein, S. O. Garbuzynskiy, 2013, Journal of biomolecular structure & dynamics.

On the Prediction of Folding Nuclei in Globular Proteins

O. V. Galzitskaya, A. Finkelstein, O. Galzitskaya, 2005, Molecular Biology.

Theoretical study of protein folding: outlining folding nuclei and estimation of protein folding rates

Sergiy O. Garbuzynskiy, Oxana V. Galzitskaya, Alexei V. Finkelstein, 2005 .

Cunning Simplicity of a Hierarchical Folding

A. Finkelstein, 2002, Journal of biomolecular structure & dynamics.

Cunning simplicity of protein folding landscapes.

A V Finkelstein, A. Finkelstein, N. S. Bogatyreva, 2001, Protein engineering.

Folding rate dependence on the chain length of RNA-like heteropolymers.

A. Finkelstein, O. Galzitskaya, 1998, Folding & design.

S6 permutein shows that the unusual target topology is not responsible for the absence of rigid tertiary structure in de novo protein albebetin

A. Finkelstein, A. Badretdinov, V. Uversky, 1997, FEBS letters.

Implications of the random characteristics of protein sequences for their three-dimensional structure

Alexei V. Finkelstein, A. Finkelstein, 1994 .

Rate of β‐structure formation in polypeptides

A. Finkelstein, A. V. Finkelstein, 1991 .

Intersubunit Mobility of the Ribosome

A. Spirin, A. Finkelstein, S. Razin, 2018, Molecular Biology.

Computer simulation of secondary structure folding of random and ‘‘edited’’ RNA chains

A. Finkelstein, O. Galzitskaya, 1996 .

Three‐state protein folding: Experimental determination of free‐energy profile

A. Finkelstein, B. Melnik, V. Bychkova, 2005, Protein science : a publication of the Protein Society.

Prediction of secondary structure, spatial organization and distribution of antigenic determinants for hepatitis A virus proteins.

A. Finkelstein, V. Mesyanzhinov, E. Peletskaya, 1987, Journal of biomolecular structure & dynamics.

Intersubunit Mobility of the Ribosome

A. Spirin, A. Finkelstein, S. Razin, 2018, Molecular Biology.

Molecular Machines in Biology: The Ribosome as a Brownian Ratchet Machine

A. Spirin, A. Finkelstein, 2011 .

Protein Engineering of Albebetin, A de Novo Protein with a Predesigned Three-Dimensional Structure

A. Finkelstein, O. Ptitsyn, M. P. Kirpichnikov, 1996 .

Recognition of signal sequences

T. Rapoport, A. Finkelstein, P. Bendzkô, 1983, FEBS Letters.

Folding intermediate and folding nucleus for I-->N and U-->I-->N transitions in apomyoglobin: contributions by conserved and nonconserved residues.

A. Finkelstein, B. Melnik, V. Bychkova, 2010, Biophysical journal.

How strong are side chain interactions in the folding intermediate?

A. Finkelstein, B. Melnik, V. Bychkova, 2009, Protein science : a publication of the Protein Society.

Anomalous Kinetics of Amyloidogenesis Suggest a Competition between Oligomers and Fibrils

A. Finkelstein, N. Dovidchenko, O. Galzitskaya, 2018, Molecular Biology.

Can protein unfolding simulate protein folding?

A V Finkelstein, A. Finkelstein, 1997, Protein engineering.

New Polarizable Atomic Force Fields for Calculation of Non-bonded Interactions in Explicit and Implicit Aqueous Surrounding

A. Finkelstein, А.В. Финкельштейн, 2010 .

Comparison of X‐ray and NMR structures: Is there a systematic difference in residue contacts between X‐ray‐ and NMR‐resolved protein structures?

M. Y. Lobanov, Oxana V Galzitskaya, Alexei V Finkelstein, 2005, Proteins.

Some peculiarities of water freezing at small sub-zero temperatures

A. Finkelstein, 2020, 2008.13682.

Optimization of Protein Structure on Lattices Using a Self-Consistent Field Approach

Jeffrey Skolnick, Alexei V. Finkelstein, Boris A. Reva, 1998, J. Comput. Biol..

Theory of protein secondary structure and algorithm of its prediction

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

Theory of protein molecule self‐organization. III. A calculating method for the probabilities of the secondary structure formation in an unfolded polypeptide chain

A V Finkelstein, A. Finkelstein, 1977, Biopolymers.

Protein structure prediction using the evolutionary algorithm USPEX

A. Finkelstein, A. Oganov, I. Kruglov, 2023, Proteins.

Intermediate states of apomyoglobin: Are they parts of the same area of conformations diagram?

A. Finkelstein, V. Bychkova, V. Balobanov, 2017, Biochemistry (Moscow).

Understanding the folding rates and folding nuclei of globular proteins.

A. Finkelstein, O. Galzitskaya, D. Ivankov, 2007, Current protein & peptide science.

Computation of biopolymers: a general approach to different problems.

A V Finkelstein, M A Roytberg, A. Finkelstein, 1993, Bio Systems.

Many-Atom van der Waals Interactions lead to Direction-Sensitive Interactions of covalent bonds

Alexei V. Finkelstein, Natalya S. Bogatyreva, Michael Y. Lobanov, 2008, J. Bioinform. Comput. Biol..

Average and extreme multi-atom Van der Waals interactions: Strong coupling of multi-atom Van der Waals interactions with covalent bonding

A. Finkelstein, 2007, Chemistry Central journal.

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.

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.

FLUCTUATING SECONDARY STRUCTURE FORMATION DURING THE FIRST STEP OF PROTEIN SELF-ORGANIZATION

A. Finkelstein, 1981 .

How Homologs Can Help to Predict Protein Folds Even Though They Cannot Be Predicted for Individual Sequences

Azat Ya. Badretdinov, Alexei V. Finkelstein, A. Finkelstein, 1998, J. Comput. Biol..

Lattice modeling: Accuracy of energy calculations

Michel F. Sanner, Arthur J. Olson, Alexei V. Finkelstein, 1996, J. Comput. Chem..

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.