Original paper
Influence of crowding agents on the dynamics of a multidomain protein in its denatured state: a solvation approach
Abstract
It is now well appreciated that the crowded intracellular environment significantly modulates an array of physiological processes including protein folding–unfolding, aggregation, and dynamics to name a few. In this work we have studied the dynamics of domain I of the protein human serum albumin (HSA) in its urea-induced denatured states, in the presence of a series of commonly used macromolecular crowding agents. HSA was labeled at Cys-34 (a...
Paper Details
Title
Influence of crowding agents on the dynamics of a multidomain protein in its denatured state: a solvation approach
Published Date
May 1, 2020
Journal
Volume
49
Issue
3-4
Pages
289 - 305
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Notes
History