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Calculation of the minimum energy conformations of Di‐, Tri‐, and tetrapeptides of glycine using a global optimization technique
Author(s) -
Rao Gita Subba,
Tyagi R. S.,
Mishra R. K.
Publication year - 2009
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/qua.560240704
Subject(s) - tripeptide , chemistry , hydrogen bond , computational chemistry , glycine , energy minimization , crystallography , thermodynamics , stereochemistry , molecule , amino acid , physics , organic chemistry , biochemistry
The preferred helical conformations of di‐, tri‐, and tetrapeptides of glycine have been calculated by the method of Subba Rao et al. [G. Subba Rao, R.S. Tyagi, and R.K. Mishra, J. Theor. Biol. 90 , 377 (1981)]. The potential function used comprises the electrostatic, nonbonded, torsional, and hydrogen bonding terms. Conformational calculations without hydrogen bonding have also been made. The results are in good agreement with those of other workers and do not depend much on the hydrogen bonding term. The tripeptide appears to be a suitable representative fragment for the conformation of polyglycine.