A Simple Approach to Analyzing Protein Side-Chain Dynamics from 13 C NMR Relaxation Data

Vladimir A. Daragan, Kevin H. Mayo

Research output: Contribution to journalEditorialpeer-review

17 Scopus citations

Abstract

A simple approach to deriving motional dynamics information of protein and peptide side chains by using 13 C NMR relaxation data is presented. By using linear approximation of internal rotational correlation functions, simple equations for relating side-chain conformation, bond rotational amplitudes, and rotational correlation coefficients with different NMR relaxation parameters have been obtained. Auto- and cross-correlation spectral densities are considered, and it is shown that proton-coupled 13 C NMR relaxation measurements allow detailed motional information to be obtained.

Original languageEnglish (US)
Pages (from-to)329-334
Number of pages6
JournalJournal of Magnetic Resonance
Volume130
Issue number2
DOIs
StatePublished - Feb 1998

Bibliographical note

Funding Information:
This work was supported by research grants from the National Science Foundation (MCB-9729539), the National Institutes of Health (AA-10806), and the North Atlantic Treaty Organization (CRG-970039).

Fingerprint Dive into the research topics of 'A Simple Approach to Analyzing Protein Side-Chain Dynamics from <sup>13</sup> C NMR Relaxation Data'. Together they form a unique fingerprint.

Cite this