Ontology highlight
ABSTRACT:
SUBMITTER: Junker JP
PROVIDER: S-EPMC1366864 | biostudies-other | 2005 Nov
REPOSITORIES: biostudies-other
Junker J P JP Hell K K Schlierf M M Neupert W W Rief M M
Biophysical journal 20050923 5
We investigated the effect of substrate binding on the mechanical stability of mouse dihydrofolate reductase using single-molecule force spectroscopy by atomic force microscopy. We find that under mechanical forces dihydrofolate reductase unfolds via a metastable intermediate with lifetimes on the millisecond timescale. Based on the measured length increase of approximately 22 nm we suggest a structure for this intermediate with intact substrate binding sites. In the presence of the substrate an ...[more]