Multiple solution conformations and internal rotations of the decapeptide gramicidin S.

摘要: The conformations of every C alpha H-C beta H2 moiety the peptide gramicidin S are reported. Internal rotation occurs, but distinct preferences for one side chain rotamer, greater than 80%, found D-phenylalanine and ornithine residues. Leucine valine exhibit more extensive averaging while proline is shown to be at least 90% in Ramachandran B conformation. data consistent with coexistence many tertiary S; statistical weights twelve major rotamer populations relative conformers depend upon temperature solvent. A comparison conclusions from this publication derived by energy minimization procedures made. Partial agreement was found, calculations have not yet predicted wealth coexisting nor accounted subtle effects It proposed that a complete picture conformational dynamics other peptides will result which use as basis reported here.