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

Vladimir A. Daragan; Kevin H. Mayo

doi:10.1006/jmre.1997.1310

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 journal › Editorial › peer-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 language	English (US)
Pages (from-to)	329-334
Number of pages	6
Journal	Journal of Magnetic Resonance
Volume	130
Issue number	2
DOIs	https://doi.org/10.1006/jmre.1997.1310
State	Published - 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).

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10.1006/jmre.1997.1310

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

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.",

author = "Daragan, {Vladimir A.} and Mayo, {Kevin H.}",

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).",

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AU - Daragan, Vladimir A.

AU - Mayo, Kevin H.

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N2 - 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.

AB - 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.

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