A Simple Approach to Analyzing Protein Side-Chain Dynamics from13C NMR Relaxation Data
โ 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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โฆ 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.
๐ SIMILAR VOLUMES
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