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 journalEditorial

17 Citations (Scopus)

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

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Protons
Nuclear magnetic resonance
proteins
Peptides
nuclear magnetic resonance
Proteins
Spectral density
Autocorrelation
correlation coefficients
cross correlation
autocorrelation
peptides
Conformations
protons
approximation

Cite this

A Simple Approach to Analyzing Protein Side-Chain Dynamics from 13 C NMR Relaxation Data . / Daragan, Vladimir A.; Mayo, Kevin H.

In: Journal of Magnetic Resonance, Vol. 130, No. 2, 02.1998, p. 329-334.

Research output: Contribution to journalEditorial

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