Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 132, Issue 32, Pages 10992-10995Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja104578n
Keywords
-
Categories
Funding
- European Molecular Biology Organization
- Canadian Institutes of Health Research (CHIR)
Ask authors/readers for more resources
A pulse scheme is presented for quantifying millisecond time scale chemical exchange processes in proteins by measuring H-1 CPMG relaxation dispersion profiles of (CHD2)-C-13 methyl groups. The use of (CHD2)-C-13 isotopomers for H-1 methyl dispersion experiments eliminates problems with interconversion between differentially relaxing proton transitions that complicate the extraction of accurate exchange parameters when (CH3)-C-13 probes are used. Good agreement is demonstrated between extracted chemical shift differences from fits of dispersion profiles and the corresponding differences measured independently on a model exchanging system, validating the experiment. The methodology is applied to the gating residues of the T. acidiphilium proteasome that are shown to undergo extensive motion on the millisecond time scale.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available