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Studies of the thyrotropin‐releasing factor. II. Conformations of TRF and some analogs
Author(s) -
Flurry R. L.,
Abdulnur S. F.,
Bopp J. M.
Publication year - 1978
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1978.360171114
Subject(s) - tautomer , chemistry , cndo/2 , protonation , stereochemistry , computational chemistry , molecule , organic chemistry , ion
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.