C-13 chemical shift tensor of L-tryptophan and its application to polypeptide structure determination

Separovic, F., Hayamizu, K., Smith, R. and Cornell, B. A. (1991) C-13 chemical shift tensor of L-tryptophan and its application to polypeptide structure determination. Chemical Physics Letters, 181 2-3: 157-162. doi:10.1016/0009-2614(91)90348-D


Author Separovic, F.
Hayamizu, K.
Smith, R.
Cornell, B. A.
Title C-13 chemical shift tensor of L-tryptophan and its application to polypeptide structure determination
Journal name Chemical Physics Letters   Check publisher's open access policy
ISSN 0009-2614
Publication date 1991-06-21
Sub-type Article (original research)
DOI 10.1016/0009-2614(91)90348-D
Open Access Status Not yet assessed
Volume 181
Issue 2-3
Start page 157
End page 162
Total pages 6
Language eng
Subject 3100 Physics and Astronomy
1606 Physical and Theoretical Chemistry
Abstract The C-13 chemical shift tensor has been determined for the indole C of tryptophan using N dipole-coupled C-13 powder spectra. σ was found to be perpendicular to the indole ring, and σ≈6° off the parallel to the NH bond. The principal values for the C-13 chemical shift tensor were found to be δ = 202, δ = 48 ppm. The results were applied to the analysis of the reduced chemical shift anisotropy obtained from C-13 enriched tryptophans in the polypeptide gramicidin A in phospholipid membranes.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
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Created: Fri, 29 Dec 2017, 06:25:50 EST