Determination of dihedral angles in peptides through experimental and theoretical studies of alpha-carbon chemical shielding tensors

TitleDetermination of dihedral angles in peptides through experimental and theoretical studies of alpha-carbon chemical shielding tensors
Publication TypeJournal Article
Year of Publication1997
AuthorsHeller J., Laws D.D, Tomaselli M., King D.S, Wemmer D.E, Pines A, Havlin R.H, Oldfield E.
JournalJournal of the American Chemical Society
Volume119
Issue33
Pagination7827-7831
Date PublishedAug 20
ISBN Number0002-7863
Accession NumberWOS:A1997XT03700025
Keywordscrystal-structure
Abstract

A simple method for the determination of backbone dihedral angles in peptides and proteins is presented. The chemical-shift anisotropies (CSA) of the central alanine alpha-carbon in powdered crystalline tripeptides, whose structures have been determined previously by X-ray crystallography, were measured by cross-polarization magic-angle-spinning nuclear magnetic resonance. The experimental CSA values were correlated with ab initio chemical-shielding calculations over Ramanchandran phi/psi space on an N-formyl-L-alanine amide fragment. Using this correlation, phi/psi probability surfaces for one of the tripeptides were calculated based only on the alpha-carbon CSA, allowing a prediction of backbone angles. Dihedral angles predicted by these calculations fall within +/-12 degrees of the values determined by crystallography. This approach should be useful in the determination of solid-slate protein structure.

URL<Go to ISI>://WOS:A1997XT03700025
DOI10.1021/Ja970124k
Short TitleDetermination of dihedral angles in peptides through experimental and theoretical studies of alpha-carbon chemical shielding tensors
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