Relative Orientation of CaHa-Bond Vectors of Successive Residues in Proteins through Cross-Correlated Relaxation in NMR

Cross-correlation between the fluctuations of 13Ca-Ha interactions affects the relaxation behavior of two-spin coherences (zero- and double-quantum coherences) involving the 13Ca nuclei of two successive amino acid residues. The cross-correlation rates are shown to depend on a dihedral angle S defined by two planes subtended by the atoms {Ha(i-1),13Ca(i-1),13Ca(i)} and {13Ca(i-1),13Ca(i),Ha(i)}. This dihedral angle is related to the secondary structure of a protein, and can be used as a constraint in various protein structure calcn. protocols. [on SciFinder (R)]


Published in:
Journal of the American Chemical Society, 122, 8, 1758-1761
Year:
2000
Laboratories:




 Record created 2006-02-22, last modified 2018-03-17


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