Temperature-dependent Hammond behavior in a protein-folding reaction: analysis of transition-state movement and ground-state effects.

ABSTRACT: Characterization of the transition-state ensemble and the nature of the free-energy barrier for protein folding are areas of intense activity and some controversy. A key issue that has emerged in recent years is the width of the free-energy barrier and the susceptibility of the transition state to movement. Here we report denaturant-induced and temperature-dependent folding studies of a small mixed alpha-beta protein, the N-terminal domain of L9 (NTL9). The folding of NTL9 was determined using fluorescence-detected stopped-flow fluorescence measurements conducted at seven different temperatures between 11 and 40 degrees C. Plots of the log of the observed first-order rate constant versus denaturant concentration, "chevron plots," displayed the characteristic V shape expected for two-state

SUBMITTER: Taskent H 

PROVIDER: S-EPMC2820404 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature