Maxim Prigozhin

Maxim Prigozhin

Harvard University

Assistant Professor

Applied Physics

Research Area

  • #Chemistry
  • #Molecular dynamics
  • #Protein folding
  • #Chemical physics
  • #Microsecond
  • #Materials science
  • #Native state
  • #Temperature jump
  • #Computational chemistry
  • #Phase diagram

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Related papers to
‘ Chemistry ‘ : 8

  • Comparing Fast Pressure Jump and Temperature Jump Protein Folding Experiments and Simulations.

    2015/06

    13.1 Impact Factor

    34 citations

    Anna Jean Wirth, Yanxin Liu, Maxim B. Prigozhin, Klaus Schulten, Martin Gruebele

    DOI : 10.1021/JACS.5B02474

    • #Chemistry
    • #Mechanics
    • #Computational chemistry
    • #Kinetics
    • #Kinetic energy
    • #Molecular dynamics
    • #Perturbation (astronomy)
    • #Protein folding
    • #Microsecond
    • #Temperature jump
    • #Pressure jump

All papers authored by
‘ Maxim Prigozhin ’ : 13

  • Comparing Fast Pressure Jump and Temperature Jump Protein Folding Experiments and Simulations.

    2015/06
    JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

    13.1 Impact Factor

    34 citations

    Anna Jean Wirth, Yanxin Liu, Maxim B. Prigozhin, Klaus Schulten, Martin Gruebele

    DOI : 10.1021/JACS.5B02474

    • #Chemistry
    • #Mechanics
    • #Computational chemistry
    • #Kinetics
    • #Kinetic energy
    • #Molecular dynamics
    • #Perturbation (astronomy)
    • #Protein folding
    • #Microsecond
    • #Temperature jump
    • #Pressure jump

Related papers to
‘ Chemistry ‘ : 8

  • Comparing Fast Pressure Jump and Temperature Jump Protein Folding Experiments and Simulations.

    2015/06
    JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

    13.1 Impact Factor

    34 citations

    Anna Jean Wirth, Yanxin Liu, Maxim B. Prigozhin, Klaus Schulten, Martin Gruebele

    DOI : 10.1021/JACS.5B02474

    • #Chemistry
    • #Mechanics
    • #Computational chemistry
    • #Kinetics
    • #Kinetic energy
    • #Molecular dynamics
    • #Perturbation (astronomy)
    • #Protein folding
    • #Microsecond
    • #Temperature jump
    • #Pressure jump
  • Criteria for Selecting PEGylation Sites on Proteins for Higher Thermodynamic and Proteolytic Stability

    2014/12
    JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

    12.1 Impact Factor

    29 citations

    Paul B. Lawrence, Yulian Gavrilov, Sam S. Matthews, Minnie I. Langlois, Dalit Shental-Bechor, Harry M. Greenblatt, Brijesh K. Pandey, Mason S. Smith, Ryan Paxman, Chad D. Torgerson, Jacob P. Merrell, Cameron C. Ritz, Maxim B. Prigozhin, Yaakov Levy, Joshua L. Price

    DOI : 10.1021/JA5095183

    • #Chemistry
    • #Biochemistry
    • #Biophysics
    • #Biological activity
    • #Side chain
    • #Oligomer
    • #Model system
    • #PEG ratio
    • #WW domain
    • #Conformational stability
    • #PEGylation

Get access to
Contact information

Log in

All papers authored by
‘ Maxim Prigozhin ’ : 13

  • Comparing Fast Pressure Jump and Temperature Jump Protein Folding Experiments and Simulations.

    2015/06
    JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

    13.1 Impact Factor

    34 citations

    Anna Jean Wirth, Yanxin Liu, Maxim B. Prigozhin, Klaus Schulten, Martin Gruebele

    DOI : 10.1021/JACS.5B02474

    • #Chemistry
    • #Mechanics
    • #Computational chemistry
    • #Kinetics
    • #Kinetic energy
    • #Molecular dynamics
    • #Perturbation (astronomy)
    • #Protein folding
    • #Microsecond
    • #Temperature jump
    • #Pressure jump
  • Criteria for Selecting PEGylation Sites on Proteins for Higher Thermodynamic and Proteolytic Stability

    2014/12
    JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

    12.1 Impact Factor

    29 citations

    Paul B. Lawrence, Yulian Gavrilov, Sam S. Matthews, Minnie I. Langlois, Dalit Shental-Bechor, Harry M. Greenblatt, Brijesh K. Pandey, Mason S. Smith, Ryan Paxman, Chad D. Torgerson, Jacob P. Merrell, Cameron C. Ritz, Maxim B. Prigozhin, Yaakov Levy, Joshua L. Price

    DOI : 10.1021/JA5095183

    • #Chemistry
    • #Biochemistry
    • #Biophysics
    • #Biological activity
    • #Side chain
    • #Oligomer
    • #Model system
    • #PEG ratio
    • #WW domain
    • #Conformational stability
    • #PEGylation

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