Ontology highlight
ABSTRACT:
SUBMITTER: Daidone I
PROVIDER: S-EPMC2799665 | biostudies-literature | 2010 Jan
REPOSITORIES: biostudies-literature
Daidone Isabella I Neuweiler Hannes H Doose Sören S Sauer Markus M Smith Jeremy C JC
PLoS computational biology 20100122 1
Characterization of the length dependence of end-to-end loop-closure kinetics in unfolded polypeptide chains provides an understanding of early steps in protein folding. Here, loop-closure in poly-glycine-serine peptides is investigated by combining single-molecule fluorescence spectroscopy with molecular dynamics simulation. For chains containing more than 10 peptide bonds loop-closing rate constants on the 20-100 nanosecond time range exhibit a power-law length dependence. However, this scalin ...[more]