Abstract
As oxidized RNase is a model for the random conformation state of RNase, the hydrogen exchange kinetics of oxidized RNase approximate the intrinsic conformation-independent chemical exchange rate of the native protein. The energy of activation, the pH min , and the k min of oxidized RNase exchange rates are similar to those reported for amino acid homopolymers. However, unlike the exchange from homopolymers, the exchange from oxidized RNase is characterized by a distribution of first-order rates. This distribution is important to the analysis of exchange from native proteins in terms of classes of sites which share common structural properties.
Dates
Type | When |
---|---|
Created | 19 years, 3 months ago (May 31, 2006, 2:21 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 10:26 a.m.) |
Indexed | 4 months, 3 weeks ago (April 5, 2025, 12:23 p.m.) |
Issued | 55 years, 1 month ago (Aug. 1, 1970) |
Published | 55 years, 1 month ago (Aug. 1, 1970) |
Published Online | 55 years, 1 month ago (Aug. 1, 1970) |
Published Print | 55 years, 1 month ago (Aug. 1, 1970) |
@article{Woodward_1970, title={OXIDIZED RNASE AS A PROTEIN MODEL HAVING NO CONTRIBUTION TO THE HYDROGEN EXCHANGE RATE FROM CONFORMATIONAL RESTRICTIONS}, volume={66}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.66.4.1067}, DOI={10.1073/pnas.66.4.1067}, number={4}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Woodward, C. K. and Rosenberg, Andreas}, year={1970}, month=aug, pages={1067–1074} }