Search Results - "Gutin, A. M"

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

“…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

“…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

“…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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Chain Length Scaling of Protein Folding Time by Gutin, AM, Abkevich, VI, VI, Shakhnovich, EI

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Implications of thermodynamics of protein folding for evolution of primary sequences by Shakhnovich, E. I, Gutin, A. M

“…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

“…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

“…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

“…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.

“…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.

“…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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Polymers with annealed and quenched branchings belong to different universality classes by Gutin, A. M, Grosberg, A. Yu, Shakhnovich, E. I

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Effect of a net charge on the conformation of polyampholytes by Gutin, AM, Shakhnovich, EI

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Influence of point mutations on protein structure: probability of a neutral mutation by Shakhnovich, E I, Gutin, A M

“…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

“…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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Microphase separation in randomly branched polymers by Gutin, A. M, Grosberg, A. Yu, Shakhnovich, E. I

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