Aggregation of pro‐leu‐gly‐NH<sub>2</sub> in aqueous solution

Walter, Roderich; Deslauriers, Roxanne; Smith, Ian C. P.

doi:10.1016/0014-5793(78)81029-1

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2009

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Cited by 9 publications

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Conformational energy calculations on the CNS-active peptide Pro-Leu-Gly-NH2

Butt

Walter

Renugopalakrishnan

et al. 2009

Int. J. Quantum Chem.

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Partitioned potential energy calculations, inclusive of hydrogen bond potential function, were performed on the molecular conformations of the endocrine-and extraendocrine-active tripeptide H-Pro-Leu-Gly-NH2. A complete search for energetically stable structures revealed the presence of type Ij3 and Ilp turn conformations, with the latter being the preferred conformation. Results of CNDO/2 molecular orbital calculations were found to be in consonance with the partitioned potential energy calculations. These data are in agreement with earlier nuclear magnetic resonance and crystallographic studies.

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