Sidechain conformational dependence of hydrogen exchange in model peptides.

Abstract

Peptide hydrogens that are exposed to solvent in protein X-ray structures exhibit a billion-fold range in hydroxide-catalyzed exchange rates, and these rates have previously been shown to be predictable by continuum dielectric methods to within a factor of 7, based on single protein conformations. When using a protein coil library to model the Boltzmann… (More)
DOI: 10.1016/j.bpc.2010.05.006

Topics

Cite this paper

@article{Anderson2010SidechainCD, title={Sidechain conformational dependence of hydrogen exchange in model peptides.}, author={Janet Anderson and G. Hern{\'a}ndez Hern{\'a}ndez and David M LeMaster}, journal={Biophysical chemistry}, year={2010}, volume={151 1-2}, pages={61-70} }