Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins.

ABSTRACT: We used single-molecule FRET in combination with other biophysical methods and molecular simulations to investigate the effect of temperature on the dimensions of unfolded proteins. With single-molecule FRET, this question can be addressed even under near-native conditions, where most molecules are folded, allowing us to probe a wide range of denaturant concentrations and temperatures. We find a compaction of the unfolded state of a small cold shock protein with increasing temperature in both the presence and the absence of denaturant, with good agreement between the results from single-molecule FRET and dynamic light scattering. Although dissociation of denaturant from the polypeptide chain with increasing temperature accounts for part of the compaction, the results indicate an important

SUBMITTER: Nettels D 

PROVIDER: S-EPMC2791578 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature