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- W89762529 abstract "Abstract The conformation of the molecule cyclo (Aha- Cys-Phe-D-Trp-Lys-Thr-Cys ) was studied by empirical conformational energy calculations. The low-energy structure found contains a type II' bend centered at the D-Trp-Lys residues. The lowest energy conformer has the aromatic ring of DTrp positioned such that the γ-protons of the Lys side-chain are in the shielding region (i.e., perpendicular to the center of the aromatic ring). This is in agreement with the NMR results. A mechanism of action for the inhibition of GH release is presented which suggests a conformational change occurs in the D-Trp side-chain ring upon binding to the receptor. The resulting structure has the Phe-D-Trp ring-ring stacking suggested to be responsible for binding and agonist activity of model growth-hormone releasing peptides." @default.
- W89762529 created "2016-06-24" @default.
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- W89762529 date "1980-07-01" @default.
- W89762529 modified "2023-10-16" @default.
- W89762529 title "Conformational energy studies of the growth hormone inhibitor, cyclo (Aha-Cys-Phe-D-Trp-Lys-Thr-Cys)" @default.
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- W89762529 doi "https://doi.org/10.1016/0006-291x(80)90704-4" @default.
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