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Dipolar Waves as NMR maps of helices in proteins.

Authors
  • Mesleh, Michael F
  • Opella, Stanley J
Type
Published Article
Journal
Journal of magnetic resonance (San Diego, Calif. : 1997)
Publication Date
Aug 01, 2003
Volume
163
Issue
2
Pages
288–299
Identifiers
PMID: 12914844
Source
Medline
License
Unknown

Abstract

Dipolar Waves describe the periodic variation in the magnitudes of dipolar couplings in the backbone of a protein as a function of residue number. They provide a direct link between experimental measurements of dipolar couplings in aligned samples and the periodicity inherent in regular secondary structure elements. It is possible to identify the residues in a helix and the type of helix, deviations from ideality, and to orient the helices relative to an external axis in completely aligned samples and relative to each other in a common frame in weakly aligned samples with Dipolar Waves. They provide a tool for accurately describing helices and a step towards high throughput structure determination of proteins.

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