Conformational properties of unfolded HypF-N.

J Phys Chem B

Department of Physics and Astronomy, Michigan State University, East Lansing, Michigan 48824, USA.

Published: December 2009

We have measured the intramolecular diffusion rate between distant residues in the aggregation-prone protein HypF-N under various denaturing conditions. Using the method of cysteine quenching of the tryptophan triplet state, we find that intramolecular diffusion remains roughly constant at high concentrations of denaturant (2-6 M GdnHCl) and slows down at low concentrations of denaturant, but the decrease is not uniform throughout the chain. Extrapolation of these measurements to 0 M GdnHCl gives D approximately 10(-7) cm(2) s(-1), about 1 order of magnitude lower than unstructured peptides and at least 2 orders of magnitude higher than well-behaved proteins. This suggests that there is a dynamic range of conformational reorganization within which partially unfolded states are prone to aggregation.

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http://dx.doi.org/10.1021/jp904189bDOI Listing

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