2015 - Fellow of American Physical Society (APS) Citation For seminal contributions to the statistical physics of polypeptides, by significantly extending methods previously used for disordered systems, and for discovery of physicalchemical principles of selection of protein sequences now used as a tool for discovery of new protein sequences
His scientific interests lie mostly in Protein folding, Folding, Phi value analysis, Native state and Crystallography. Eugene I. Shakhnovich combines subjects such as Chemical physics, Thermodynamics, Statistical physics, Protein structure and Levinthal's paradox with his study of Protein folding. Eugene I. Shakhnovich interconnects Helix, Cooperativity, Gene and Lattice monte carlo in the investigation of issues within Folding.
His Phi value analysis research includes elements of Contact order and Nucleus. His Native state study incorporates themes from Random coil, Protein engineering and Biological system. His study looks at the intersection of Crystallography and topics like Molecular dynamics with Globular protein.
Eugene I. Shakhnovich mainly focuses on Protein folding, Statistical physics, Protein structure, Genetics and Folding. His work deals with themes such as Crystallography, Native state and Chemical physics, which intersect with Protein folding. In most of his Statistical physics studies, his work intersects topics such as Monte Carlo method.
As part of his studies on Protein structure, Eugene I. Shakhnovich often connects relevant areas like Computational biology. His Genetics study combines topics from a wide range of disciplines, such as Evolutionary biology and Fitness landscape. His Contact order study integrates concerns from other disciplines, such as Lattice protein and Downhill folding.
Biophysics, Protein folding, Dihydrofolate reductase, Mutant and Crystallin are his primary areas of study. His Biophysics research integrates issues from Protein aggregation, Disulfide bond, Folding, Substrate and Adenylate kinase. His research integrates issues of Protein structure and Protein domain in his study of Protein folding.
His Dihydrofolate reductase research also works with subjects such as
His main research concerns Biophysics, Protein folding, Genetics, Gene and Evolutionary ecology. The concepts of his Biophysics study are interwoven with issues in Mutant, Crystallin, Adenylate kinase and Substrate. Eugene I. Shakhnovich has researched Protein folding in several fields, including Protein structure, Protein domain, Computational biology and Protein aggregation.
His study on Lineage, Hemagglutinin, Influenza vaccine and Nucleoprotein is often connected to Selective sweep as part of broader study in Genetics. The study incorporates disciplines such as Contact order, Native structure and Translocon in addition to Gene. He has included themes like Range and Competition in his Evolutionary ecology study.
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How does a protein fold
Andrej Šali;Eugene Shakhnovich;Martin Karplus.
Kinetics of protein folding. A lattice model study of the requirements for folding to the native state.
Andrej Šali;Eugene Shakhnovich;Martin Karplus.
Journal of Molecular Biology (1994)
Engineering of stable and fast-folding sequences of model proteins
E I Shakhnovich;A M Gutin.
Proceedings of the National Academy of Sciences of the United States of America (1993)
Specific nucleus as the transition state for protein folding: evidence from the lattice model.
V. I. Abkevich;A. M. Gutin;E. I. Shakhnovich.
On the transition coordinate for protein folding
Rose Du;Vijay S. Pande;Vijay S. Pande;Alexander Yu. Grosberg;Toyoichi Tanaka.
Journal of Chemical Physics (1998)
Theoretical studies of protein-folding thermodynamics and kinetics.
Eugene I Shakhnovich.
Current Opinion in Structural Biology (1997)
Proteins with selected sequences fold into unique native conformation.
Physical Review Letters (1994)
Conserved residues and the mechanism of protein folding
E. Shakhnovich;V. Abkevich;O. Ptitsyn.
The role of topological constraints in the kinetics of collapse of macromolecules
A. Yu. Grosberg;S.K. Nechaev;E.I. Shakhnovich.
Journal De Physique (1988)
Universally conserved positions in protein folds: reading evolutionary signals about stability, folding kinetics and function.
Leonid A. Mirny;Eugene I. Shakhnovich.
Journal of Molecular Biology (1999)
Profile was last updated on December 6th, 2021.
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