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Study of the conformational profile of selected unnatural amino acid residues derived from l ‐phenylalanine
Author(s) -
GomezCatalan Jesus,
Perez Juan J.,
Jimenez Ana I.,
Cativiela Carlos
Publication year - 1999
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/(sici)1099-1387(199906)5:6<251::aid-psc190>3.0.co;2-k
Subject(s) - dipeptide , ramachandran plot , chemistry , molecular mechanics , stereochemistry , amino acid , phenylalanine , peptide , protein structure , molecular dynamics , computational chemistry , biochemistry
The present work reports the results of a conformational study performed on seven unnatural amino acid residues and on its natural precursor, investigated by means of computational methods at the molecular mechanics level. Amino acid residues selected for the present study are derivatives of l ‐phenylalanine substituted at the α and/or β carbons. This series is composed of different linear analogs, including α‐methyl, β‐methyl and β‐phenyl substituted with different stereochemistry. Analysis of the Ramachandran maps of the corresponding dipeptides in vacuo reveals their conformational preferences, to be used as guidance for the synthesis of constrained peptide analogs with desired conformational propensities. The available conformational space for every dipeptide is also analysed. Copyright © 1999 European Peptide Society and John Wiley & Sons, Ltd.