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A Simple Approach to Analyzing Protein Side-Chain Dynamics from13C NMR Relaxation Data

โœ Scribed by Vladimir A. Daragan; Kevin H. Mayo


Publisher
Elsevier Science
Year
1998
Tongue
English
Weight
181 KB
Volume
130
Category
Article
ISSN
1090-7807

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โœฆ Synopsis


A simple approach to deriving motional dynamics information of protein and peptide side chains by using 13C 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 13C NMR relaxation measurements allow detailed motional information to be obtained.


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โœ Dmitri V. Mikhailov; Lais Washington; Alexei M. Voloshin; Vladimir A. Daragan; K ๐Ÿ“‚ Article ๐Ÿ“… 1999 ๐Ÿ› Wiley (John Wiley & Sons) ๐ŸŒ English โš– 131 KB ๐Ÿ‘ 1 views

The study of backbone and side-chain internal motions in proteins and peptides is crucial to having a better understanding of protein/peptide "structure" and to characterizing unfolded and partially folded states of proteins and peptides. To achieve this, however, requires establishing a baseline fo