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Eugene I. Shakhnovich

Eugene I. Shakhnovich

D-Index & Metrics

Chemistry

D-Index
87
Citations
28505
World Ranking
2396
National Ranking
848

Research.com Recognitions

  • 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

Overview

Eugene I. Shakhnovich is affiliated with Harvard University in the United States. Their research primarily spans the field of Biochemistry, Genetics and Molecular Biology, with a significant focus on Molecular Biology, Materials Chemistry, Genetics, Infectious Diseases, and Computational Theory and Mathematics.

Their scholarly work covers a range of topics, notably:

  • Protein Structure and Dynamics
  • RNA and protein synthesis mechanisms
  • RNA Research and Splicing
  • Enzyme Structure and Function
  • Connexins and lens biology
  • Evolution and Genetic Dynamics
  • RNA modifications and cancer

Shakhnovich has contributed extensively to scientific literature with frequent publications in several venues, including:

  • bioRxiv (Cold Spring Harbor Laboratory)
  • Biophysical Journal
  • arXiv (Cornell University)
  • Proceedings of the National Academy of Sciences
  • Nature Communications

Recent notable papers include:

  • "Dynamic metastable long-living droplets formed by sticker-spacer proteins" (2020, eLife)
  • "Cotranslational folding allows misfolding-prone proteins to circumvent deep kinetic traps" (2020, Proceedings of the National Academy of Sciences)
  • "The physics of liquid-to-solid transitions in multi-domain protein condensates" (2022, Biophysical Journal)
  • "Thermal Half-Lives of Azobenzene Derivatives: Virtual Screening Based on Intersystem Crossing Using a Machine Learning Potential" (2023, ACS Central Science)
  • "Phosphorylation sites are evolutionary checkpoints against liquid-solid transition in protein condensates" (2023, Proceedings of the National Academy of Sciences)

Frequent collaborators in Shakhnovich's research include Eugene Serebryany, Srivastav Ranganathan, D. I. C. Wang, Amir Bitran, and Sourav Chowdhury.

In recognition of their work, Eugene I. Shakhnovich was named a Fellow of the American Physical Society (APS) in 2015. The citation highlighted contributions to the statistical physics of polypeptides, advancement of methods for disordered systems, and discoveries related to physical-chemical principles guiding protein sequence selection.

Best Publications

  • 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

  • Engineering of stable and fast-folding sequences of model proteins

    E I Shakhnovich;A M Gutin

  • Specific nucleus as the transition state for protein folding: evidence from the lattice model.

    V. I. Abkevich;A. M. Gutin;E. I. Shakhnovich

  • Common activation mechanism of class A GPCRs.

    Qingtong Zhou;Dehua Yang;Meng Wu;Meng Wu;Yu Guo;Yu Guo

  • On the transition coordinate for protein folding

    Rose Du;Vijay S. Pande;Vijay S. Pande;Alexander Yu. Grosberg;Toyoichi Tanaka

  • The role of topological constraints in the kinetics of collapse of macromolecules

    A. Yu. Grosberg;S.K. Nechaev;E.I. Shakhnovich

  • Theoretical studies of protein-folding thermodynamics and kinetics.

    Eugene I Shakhnovich

  • Proteins with selected sequences fold into unique native conformation.

    Shakhnovich Ei

  • Estimating the Entropic Cost of Self-Assembly of Multiparticle Hydrogen-Bonded Aggregates Based on the Cyanuric Acid·Melamine Lattice

    Mathai Mammen;Eugene I. Shakhnovich;John M. Deutch;George M. Whitesides

  • Conserved residues and the mechanism of protein folding

    E. Shakhnovich;V. Abkevich;O. Ptitsyn

  • Universally conserved positions in protein folds: reading evolutionary signals about stability, folding kinetics and function.

    Leonid A. Mirny;Eugene I. Shakhnovich

  • Protein folding theory: from lattice to all-atom models.

    Leonid Mirny;Eugene Shakhnovich

  • Protein Folding Thermodynamics and Dynamics: Where Physics, Chemistry, and Biology Meet

    Eugene I Shakhnovich

  • Formation of unique structure in polypeptide chains theoretical investigation with the aid of a replica approach

    E.I. Shakhnovich;A.M. Gutin

  • SMoG: de Novo Design Method Based on Simple, Fast, and Accurate Free Energy Estimates. 1. Methodology and Supporting Evidence

    Robert S. DeWitte;Eugene I. Shakhnovich

  • Discrete molecular dynamics studies of the folding of a protein-like model.

    Nikolay V. Dokholyan;Sergey V. Buldyrev;H Eugene Stanley;Eugene I. Shakhnovich

  • Impact of local and non-local interactions on thermodynamics and kinetics of protein folding.

    V.I. Abkevich;A.M. Gutin;E.I. Shakhnovich

  • Protein folding bottlenecks: A lattice Monte Carlo simulation.

    E. Shakhnovich;G. Farztdinov;A. M. Gutin;M. Karplus

  • Topological determinants of protein folding

    Nikolay V. Dokholyan;Lewyn Li;Feng Ding;Eugene I. Shakhnovich

  • Implications of thermodynamics of protein folding for evolution of primary sequences.

    E. I. Shakhnovich;E. I. Shakhnovich;A. M. Gutin

  • How to derive a protein folding potential? A new approach to an old problem.

    Leonid A. Mirny;Eugene I. Shakhnovich

Frequent Co-Authors

Nikolay V. Dokholyan
Nikolay V. Dokholyan Pennsylvania State University
Sergey V. Buldyrev
Sergey V. Buldyrev Yeshiva University
Martin Karplus
Martin Karplus Harvard University
H. Eugene Stanley
H. Eugene Stanley Boston University
Feng Ding
Feng Ding Clemson University
Ricardo A. Broglia
Ricardo A. Broglia University of Milan
Andrej Sali
Andrej Sali University of California, San Francisco
George M. Whitesides
George M. Whitesides Harvard University

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