Ontology highlight
ABSTRACT:
SUBMITTER: Rajabi K
PROVIDER: S-EPMC4534179 | biostudies-literature | 2015 Aug
REPOSITORIES: biostudies-literature
Rajabi Khadijeh K Reuther Julia J Deuerling Elke E Radford Sheena E SE Ashcroft Alison E AE
Protein science : a publication of the Protein Society 20150611 8
The kinetics and thermodynamics of protein folding are commonly studied in vitro by denaturing/renaturing intact protein sequences. How these folding mechanisms relate to de novo folding that occurs as the nascent polypeptide emerges from the ribosome is much less well understood. Here, we have employed limited proteolysis followed by mass spectrometry analyses to compare directly free and ribosome-tethered polypeptide chains of the Src-homology 3 (SH3) domain and its unfolded variant, SH3-m10. ...[more]