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: Measurement of 15N-T1 relaxation rates in a perdeuterated protein by magic angle spinning solid-state nuclear magnetic resonance spectroscopy.
    Author: Chevelkov V, Diehl A, Reif B.
    Journal: J Chem Phys; 2008 Feb 07; 128(5):052316. PubMed ID: 18266433.
    Abstract:
    In this paper, we present the measurement of (15)N-T(1) relaxation times in the solid state for a perdeuterated protein for which exchangeable protons are back substituted during recrystallization using a buffer which contains 10% H(2)O and 90% D(2)O. We find large variations of the (15)N relaxation time, even within the same beta sheet. By comparing (15)N-T(1) relaxation times measured for a protonated and a deuterated protein (using the above mentioned approach), we conclude that (1)H driven (15)N,(15)N spin diffusion has a significant impact on the absolute (15)N relaxation time in protonated proteins. This effect is important for a quantitative analysis of relaxation data in terms of molecular dynamics.
    [Abstract] [Full Text] [Related] [New Search]