Ontology highlight
ABSTRACT:
SUBMITTER: Muller-Spath S
PROVIDER: S-EPMC2930438 | biostudies-literature | 2010 Aug
REPOSITORIES: biostudies-literature
Müller-Späth Sonja S Soranno Andrea A Hirschfeld Verena V Hofmann Hagen H Rüegger Stefan S Reymond Luc L Nettels Daniel D Schuler Benjamin B
Proceedings of the National Academy of Sciences of the United States of America 20100716 33
Many eukaryotic proteins are disordered under physiological conditions, and fold into ordered structures only on binding to their cellular targets. Such intrinsically disordered proteins (IDPs) often contain a large fraction of charged amino acids. Here, we use single-molecule Förster resonance energy transfer to investigate the influence of charged residues on the dimensions of unfolded and intrinsically disordered proteins. We find that, in contrast to the compact unfolded conformations that h ...[more]