Valeri Barsegov
University of Massachusetts Lowell
86 Papers
357 Citations
Valeri Barsegov is an academic researcher from University of Massachusetts Lowell. The author has contributed to research in topics: Chemistry & Fibrin. The author has an hindex of 21, co-authored 73 publications. Previous affiliations of Valeri Barsegov include University of Maryland, College Park & University of Rochester.
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Papers
Dynamics of unbinding of cell adhesion molecules: Transition from catch to slip bonds
Valeri Barsegov,D. Thirumalai +1 more
TL;DR: A model that considers the possibility of redistribution of population from one force-free state to another force-stabilized bound state is used to compute the distributions of unbinding times and unbinding forces as a function of the loading rate, rf.
Mechanism of Fibrin(ogen) Forced Unfolding
Artem Zhmurov,Artem Zhmurov,André Ex Brown,Rustem I. Litvinov,Ruxandra I. Dima,John W. Weisel,Valeri Barsegov,Valeri Barsegov +7 more
TL;DR: It is found that mechanical unraveling of fibrin(ogen) is determined by the combined molecular transitions that couple stepwise unfolding of the γ chain nodules and reversible extension-contraction of the α-helical coiled-coil connectors.
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Mechanical transition from α-helical coiled coils to β-sheets in fibrin(ogen).
Artem Zhmurov,Olga Kononova,Olga Kononova,Rustem I. Litvinov,Ruxandra I. Dima,Valeri Barsegov,Valeri Barsegov,John W. Weisel +7 more
TL;DR: The soft α-to-β phase transition in coiled coil connectors of the human fibrin(ogen) molecule might be a universal mechanism underlying mechanical properties of filamentous α-helical proteins.
Sop‐GPU: Accelerating biomolecular simulations in the centisecond timescale using graphics processors
Artem Zhmurov,Artem Zhmurov,Ruxandra I. Dima,Yaroslav Kholodov,Valeri Barsegov,Valeri Barsegov +5 more
TL;DR: It is found that the mechanical molecular response critically depends on the conditions of force application and that the kinetics and pathways for unfolding change drastically even upon a modest 10‐fold increase in vf, implying that, to resolve accurately the free energy landscape and to relate the results of single‐molecule experiments in vitro and in silico, molecular simulations should be carried out under the experimentally relevant force loads.
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Tubulin bond energies and microtubule biomechanics determined from nanoindentation in silico.
Olga Kononova,Olga Kononova,Yaroslav Kholodov,Kelly E. Theisen,Kenneth A. Marx,Ruxandra I. Dima,Fazly I. Ataullakhanov,Fazly I. Ataullakhanov,Ekaterina L. Grishchuk,Valeri Barsegov,Valeri Barsegov +10 more
TL;DR: In this article, a microtubule is modeled as a system of rigid elements interconnected through a network of lateral and longitudinal elastic bonds, and the free energies of dissociation of the tubulin-tubulin bonds are determined.
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