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An investigation of contributions to carbon-13 spin-lattice relaxtion in amino acids and peptide hormones

✍ Scribed by J. D. Cutnell; Jay A. Glasel; V. J. Hruby

Publisher: John Wiley and Sons
Year: 1975
Tongue: English
Weight: 802 KB
Volume: 7
Category: Article
ISSN: 0749-1581
DOI: 10.1002/mrc.1270070603

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✦ Synopsis

Abstract

Carbon‐13 spin‐lattice relaxation times have been measured in glycine and the tripeptide pro‐leu‐gly‐NH~2~. These times are compared with those measured in the same compounds where the glycine α‐carbon has been deuterated. In this manner evidence is obtained which indicates that mechanisms other than dipolar interactions with covalently bonded protons may contribute to carbon‐13 spin‐lattice relaxation. The effect of these additional mechanisms is found to be non‐negligible for the carbonyl carbon of glycine and the glycine α‐carbon of the tripeptide. The implication of these findings for deducing motional information from carbon‐13 relaxation measurements is briefly discussed.

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✍ Jinping Tian; Yingwu Yin 📂 Article 📅 2004 🏛 John Wiley and Sons 🌐 English ⚖ 132 KB

## Measurements of the enhancement, by various electrolytes, of the spin-lattice relaxation time of carbon-13 at different locations in a number of amino acids are reported. Spin-lattice relaxation times T 1 of all the carbons in amino acids generally tend to decrease with increase in the concentr