Search Results - "Gutin, A M"

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    Engineering of Stable and Fast-Folding Sequences of Model Proteins by Shakhnovich, E. I., Gutin, A. M.

    “…The statistical mechanics of protein folding implies that the best-folding proteins are those that have the native conformation as a pronounced energy minimum…”
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    Specific Nucleus as the Transition State for Protein Folding: Evidence from the Lattice Model by Abkevich, V. I, Gutin, A. M, Shakhnovich, E. I

    Published in Biochemistry (Easton) (01-08-1994)
    “…We have studied the folding mechanism of lattice model 36-mer proteins. Using a simulated annealing procedure in sequence space, we have designed sequences to…”
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    Protein folding Bottlenecks : a lattice Monte Carlo simulation by SHAKHNOVICH, E, FARZTCDINOV, G, GUTIN, A. M, KARPLUS, M

    Published in Physical review letters (16-09-1991)
    “…Results of Monte Carlo simulations of folding of a model "protein," which is a freely joined 27-monomer chain on a simple cubic lattice with nearest-neighbor…”
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    Is Burst Hydrophobic Collapse Necessary for Protein Folding? by Gutin, A. M, Abkevich, V. I, Shakhnovich, E. I

    Published in Biochemistry (Easton) (07-03-1995)
    “…Folding of the lattice model of proteins is studied using Monte Carlo simulation. The amino acid sequence is designed to have a pronounced energy minimum for a…”
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    Implications of thermodynamics of protein folding for evolution of primary sequences by Shakhnovich, E. I, Gutin, A. M

    Published in Nature (London) (23-08-1990)
    “…Natural proteins exhibit essentially two-state thermodynamics, with one stable fold that dominates thermodynamically over a vast number of possible folds, a…”
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    A new approach to the design of stable proteins by Shakhnovich, E I, Gutin, A M

    Published in Protein engineering (01-11-1993)
    “…We propose a simple algorithm to design a sequence which fits a given protein structure with a given energy. The algorithm is a modification of the Metropolis…”
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    Evolution-Like Selection of Fast-Folding Model Proteins by Gutin, A. M., Abkevich, V. I., Shakhnovich, E. I.

    “…We propose an algorithm providing sequences of model proteins with rapid folding into a given target (native) conformation. This algorithm is applied to a…”
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    Formation of unique structure in polypeptide chains. Theoretical investigation with the aid of a replica approach by Shakhnovich, E I, Gutin, A M

    Published in Biophysical chemistry (01-11-1989)
    “…A replica approach analogous to that used in spin glass systems is implemented to study the configurational space of a heteropolymeric model of protein with a…”
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    How the First Biopolymers Could have Evolved by Abkevich, V. I., Gutin, A. M., Shakhnovich, E. I.

    “…In this work, we discuss a possible origin of the first biopolymers with stable unique structures. We suggest that at the prebiotic stage of evolution, long…”
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    Simulations of Chaperone-Assisted Folding by Sfatos, C. D, Gutin, A. M, Abkevich, V. I, Shakhnovich, E. I

    Published in Biochemistry (Easton) (09-01-1996)
    “…We investigated a chaperone mechanism of protein folding using a 36-mer model on a cubic lattice. The mechanism simulates folding, which proceeds with…”
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    Impact of Local and Non-local Interactions on Thermodynamics and Kinetics of Protein Folding by Abkevich, V.I., Gutin, A.M., Shakhnovich, E.I.

    Published in Journal of molecular biology (29-09-1995)
    “…To address the question of how the geometry of a protein's native conformation affects its folding and stability, we studied three model 36-mers on a cubic…”
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    Domains in folding of model proteins by Abkevich, V.I., Gutin, A.M., Shakhnovich, E.I.

    Published in Protein science (01-06-1995)
    “…By means of Monte Carlo simulation, we investigated the equilibrium between folded and unfolded states of lattice model proteins. The amino acid sequences were…”
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    Influence of point mutations on protein structure: probability of a neutral mutation by Shakhnovich, E I, Gutin, A M

    Published in Journal of theoretical biology (21-04-1991)
    “…We investigate the probability X that a random mutation (i.e. the substitution in a random site of one amino acid residue by randomly chosen residue) will be a…”
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    Two slow stages in refolding of bovine carbonic anhydrase B are due to proline isomerization by Semisotnov, G V, Uversky, V N, Sokolovsky, I V, Gutin, A M, Razgulyaev, O I, Rodionova, N A

    Published in Journal of molecular biology (05-06-1990)
    “…Kinetics of refolding of bovine carbonic anhydrase B have been studied by the "double-jump" technique (i.e. the dependence of protein refolding on delay time…”
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    Why do protein architectures have Boltzmann-like statistics? by Finkelstein, A V, Badretdinov AYa, Gutin, A M

    “…A theoretical study has shown that the occurrence of various structural elements in stable folds of random copolymers is exponentially dependent on the own…”
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    Theory of kinetic partitioning in protein folding with possible applications to prions by Abkevich, V.I., Gutin, A.M., Shakhnovich, E.I.

    “…This study focuses on the phenomenon of kinetic partitioning when a polypeptide chain has two ground‐state conformations, one of which is kinetically more…”
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