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Studies of the thyrotropin-releasing factor. II. Conformations of TRF and some analogs

✍ Scribed by R. L. Flurry JR.; S. F. Abdulnur; J. M. Bopp JR.

Publisher
Wiley (John Wiley & Sons)
Year
1978
Tongue
English
Weight
404 KB
Volume
17
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

The conformation of the thyrotropin‐releasing factor (TRF) and four analogs have been studied by the CNDO/2 molecular orbital method. The N^δ^‐protonated tautomer of TRF is predicted to be the more stable of the two tautomeric forms; however, it is postulated that the N^ε^‐tautomer possesses the most active minimum‐energy conformation. The peptide backbone for the five compounds remains nearly constant. The conformations predicted from model fragments are very near to those found for the full compound.

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