Ontology highlight
ABSTRACT:
SUBMITTER: Meuzelaar H
PROVIDER: S-EPMC3948500 | biostudies-literature | 2014 Mar
REPOSITORIES: biostudies-literature
Meuzelaar Heleen H Tros Martijn M Huerta-Viga Adriana A van Dijk Chris N CN Vreede Jocelyne J Woutersen Sander S
The journal of physical chemistry letters 20140214 5
Salt bridges are known to play an essential role in the thermodynamic stability of the folded conformation of many proteins, but their influence on the <i>kinetics</i> of folding remains largely unknown. Here, we investigate the effect of Glu-Arg salt bridges on the kinetics of α-helix folding using temperature-jump transient-infrared spectroscopy and steady-state UV circular dichroism. We find that geometrically optimized salt bridges (Glu<sup>-</sup> and Arg<sup>+</sup> are spaced four peptide ...[more]