Relative Orientation of Peptide Planes in Proteins Is Reflected in Carbonyl−Carbonyl Chemical Shift Anisotropy Cross-Correlated Spin Relaxation

Autor:	Robert Konrat, Nikolai R. Skrynnikov, D. R. Muhandiram, Lewis E. Kay
Rok vydání:	2000
Předmět:	chemistry.chemical_classification Quantitative Biology::Biomolecules Spins Chemistry Hydrogen bond Relaxation (NMR) Peptide General Chemistry Dihedral angle Biochemistry Catalysis SH3 domain Crystallography Colloid and Surface Chemistry Spectrin Anisotropy
Zdroj:	Journal of the American Chemical Society. 122:7059-7071
ISSN:	1520-5126 0002-7863
DOI:	10.1021/ja0000201
Popis:	Experiments for measuring chemical shift anisotropy (CSA) cross-correlated spin relaxation between pairs of carbonyl spins in 15 N, 13 C-labeled proteins based on differences in relaxation rates of double- and zero-quantum carbonyl coherences are presented. In the case where the carbonyl spins reside on successive residues, information about the intervening (,a) backbone dihedral angles is obtained. A good correlation between predicted and measured cross-correlation rates is observed in experiments recorded on an SH3 domain from spectrin. Cross-correlated spin relaxation between carbonyl spins residing on two peptide planes linked via hydrogen bonding can also be measured for small proteins in concentrated samples, providing information about the relative orientation of these planes, as demonstrated for the spectrin SH3 domain.
Databáze:	OpenAIRE
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