R. Vavrin
Paul Scherrer Institute
9 Papers
70 Citations
R. Vavrin is an academic researcher from Paul Scherrer Institute. The author has contributed to research in topics: Small-angle neutron scattering & Dynamic light scattering. The author has an hindex of 5, co-authored 9 publications.
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Papers
Surfactant-induced protein unfolding as studied by small-angle neutron scattering and dynamic light scattering
TL;DR: In this article, the structural changes of protein bovine serum albumin (BSA) during its unfolding on the addition of anionic surfactant sodium dodecyl sulfate (SDS) have been studied using small-angle neutron scattering (SANS) and dynamic light scattering (DLS).
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Structural evolution during protein denaturation as induced by different methods
TL;DR: It is shown structure of the protein-surfactant complex can be stabilized at higher temperatures, which is not the case for pure protein.
Structural study of coacervation in protein-polyelectrolyte complexes
TL;DR: Coacervation is a dense liquid-liquid phase separation and herein it is reported coacervation of protein bovine serum albumin (BSA) in the presence of polyelectrolyte sodium polystyrene sulfonate (NaPSS) under varying solution conditions.
Small-angle neutron scattering study of structure and kinetics of temperature-induced protein gelation.
TL;DR: The phase diagram, structural evolution, and kinetics of temperature-induced protein gelation of protein Bovine Serum Albumin have been studied as a function of solution pH and protein concentration and the structure of the protein molecule remains stable up to temperatures very close to the gelation temperature.
Small-angle neutron scattering study of protein unfolding and refolding
TL;DR: The dilution method is used to show the refolding of unfolded proteins in the presence of urea and surfactant and the protein unfolding is shown to be reversible in all the above denaturating methods.