These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Observation and relaxation properties of individual fast-relaxing proton transitions in [¹³CH₃]-methyl-labeled, deuterated proteins.
    Author: Sun H, Tugarinov V.
    Journal: J Magn Reson; 2012 Apr; 217():100-5. PubMed ID: 22425372.
    Abstract:
    A pair of NMR experiments is developed for separation of individual fast-relaxing transitions in (13)CH(3) methyl groups of methyl-protonated, highly deuterated proteins, and the measurement of their relaxation rates. Intra-methyl (1)H-(1)H/(1)H-(13)C dipole-dipole cross-correlated spin relaxation that differentiates the rates of the fast-relaxing transitions depending on the state of (13)C spins, is measured in the selectively [(13)CH(3)]-methyl-labeled, deuterated ubiquitin at 10, 27, and 40°C. In contrast with previous observations, the (1)H-(1)H/(1)H-(13)C cross-correlated relaxation rates measured from relaxation rates of single-quantum proton transitions serve as good measures of side-chain order even in proteins with global rotational correlation times significantly less than 10 ns.
    [Abstract] [Full Text] [Related] [New Search]