E
Eugene I. Shakhnovich
Researcher at Harvard University
Publications - 473
Citations - 26389
Eugene I. Shakhnovich is an academic researcher from Harvard University. The author has contributed to research in topics: Protein folding & Folding (chemistry). The author has an hindex of 82, co-authored 454 publications receiving 24773 citations. Previous affiliations of Eugene I. Shakhnovich include University of Pennsylvania & Russian Academy of Sciences.
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Is catalytic activity of chaperones a selectable trait for the emergence of heat shock response
TL;DR: It is found that only cells expressing foldase chaperones are capable of genuine heat shock response to the increase in the amount of unfolded proteins at elevated temperatures, and evolutionary dynamics for two models of chaperon action are compared and contrast.
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Orientational Ordering in Sequence-Disordered Liquid Crystalline Polymers
TL;DR: In this article, the phase separation of sequence-disordered liquid crystalline polymers, a promising class of technological and biological relevance, is studied by field theory, and thermodynamic mechanisms responsible for orientational ordering observed in experiments.
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From Knowledge‐Based Potentials to Combinatorial Lead Design in Silico
TL;DR: Combinatorial small molecule growth (CombiSMoG) as discussed by the authors is based on two components: a fast and accurate knowledge-based scoring function used to predict binding affinities of protein-ligand complexes, and a Monte Carlo combinatorial growth algorithm that generates large numbers of low-free-energy ligands in the binding site of a protein.
Posted ContentDOI
Metabolic response to point mutations reveals principles of modulation of in vivo enzyme activity and phenotype
TL;DR: In this article, the authors use metabolomic analysis to elucidate the molecular mechanism underlying the filamentous phenotype of E. coli strains that carry destabilizing mutations in Dihydrofolate Reductase (DHFR).
Posted ContentDOI
Conformational catalysis of cataract-associated aggregation by interacting intermediates in a human eye lens crystallin
TL;DR: In this article, an early unfolding intermediate with an opened domain interface is proposed, which enables transient dimerization of WT and mutant, or mutant and mutant H{gamma}D molecules at their C-terminal domains.