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- Barsegov, Valeri, et al. Show all 9 Authors
- The Journal of physical chemistry 2017 v.121 no.33 pp. 7833-7843
- activation energy; blood coagulation; blood plasma; diffusivity; fibrin; fibrinogen; hydrodynamics; models; molecular dynamics; polymerization; temperature
- ... We studied the hydrodynamic behavior of fibrinogen, a blood plasma protein involved in blood clotting, in a broad 0.3–60 mg/mL range of concentration and 5–42 °C temperature using pulsed-field gradient ¹H NMR-diffusometry. Arrhenius plots revealed the activation energy for fibrinogen diffusion Ed = 21.3 kJ/mol at 1.4 mg/mL and 28.4 kJ/mol at 38 mg/mL. We found a dramatic slowdown in fibrinogen sel ...
- Barsegov, Valeri, et al. Show all 5 Authors
- Journal of the American Chemical Society 2017 v.139 no.45 pp. 16168-16177
- biocompatible materials; chemotaxis; fibrin; myosin; phase transition; phenylalanine; plastic deformation; plasticity; polypeptides; strength (mechanics); topology; vimentin
- ... We carried out dynamic force manipulations in silico on a variety of coiled-coil protein fragments from myosin, chemotaxis receptor, vimentin, fibrin, and phenylalanine zippers that vary in size and topology of their α-helical packing. When stretched along the superhelical axis, all superhelices show elastic, plastic, and inelastic elongation regimes and undergo a dynamic transition from the α-hel ...
- Barsegov, Valeri, et al. Show all 7 Authors
- Biochemistry 2017 v.56 no.13 pp. 1932-1942
- Gibbs free energy; fibrin; fibrinogen; integrins; molecular models; peptides; platelet aggregation
- ... Binding of soluble fibrinogen to the activated conformation of the integrin αIIbβ3 is required for platelet aggregation and is mediated exclusively by the C-terminal AGDV-containing dodecapeptide (γC-12) sequence of the fibrinogen γ chain. However, peptides containing the Arg-Gly-Asp (RGD) sequences located in two places in the fibrinogen Aα chain inhibit soluble fibrinogen binding to αIIbβ3 and m ...
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