Ontology highlight
ABSTRACT:
SUBMITTER: Margittai M
PROVIDER: S-EPMC307599 | biostudies-literature | 2003 Dec
REPOSITORIES: biostudies-literature
Margittai M M Widengren J J Schweinberger E E Schröder G F GF Felekyan S S Haustein E E König M M Fasshauer D D Grubmüller H H Jahn R R Seidel C A M CA
Proceedings of the National Academy of Sciences of the United States of America 20031210 26
Protein conformational transitions form the molecular basis of many cellular processes, such as signal transduction and membrane traffic. However, in many cases, little is known about their structural dynamics. Here we have used dynamic single-molecule fluorescence to study at high time resolution, conformational transitions of syntaxin 1, a soluble N-ethylmaleimide-sensitive factor attachment protein receptors protein essential for exocytotic membrane fusion. Sets of syntaxin double mutants wer ...[more]