Ontology highlight
ABSTRACT:
SUBMITTER: Hu KN
PROVIDER: S-EPMC2805027 | biostudies-literature | 2010 Jan
REPOSITORIES: biostudies-literature
Hu Kan-Nian KN Yau Wai-Ming WM Tycko Robert R
Journal of the American Chemical Society 20100101 1
We describe the use of solid-state NMR spectroscopy to characterize a partially folded state of the 35-residue helical protein HP35 created by rapid freeze-quenching from a thermally unfolded state on the 10-20 micros time scale. Two-dimensional solid-state (13)C NMR spectra of (13)C-labeled HP35 in frozen glycerol/water solution exhibit two sets of signals, one corresponding to strongly unfolded protein molecules and the other to an ensemble of molecules having native helical secondary structur ...[more]