Residue Requirements for Helical Folding in Short α/β-Peptides:  Crystallographic Characterization of the 11-Helix in an Optimized Sequence

Design of functional foldamers requires knowledge of the conformational propensities of constituent residues. Here, we explore the effects of variations in both α-amino acid and β-amino acid substitution on α/β-peptide helicity. We also report the first X-ray crystal structure of a helical α/β-pepti...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2005-09, Vol.127 (38), p.13130-13131
Main Authors: Schmitt, Margaret A, Choi, Soo Hyuk, Guzei, Ilia A, Gellman, Samuel H
Format: Article
Language:English
Subjects:
Biological and medical sciences
Carbohydrate Sequence
Conformational dynamics in molecular biology
Crystallography
Crystallography, X-Ray
Fundamental and applied biological sciences. Psychology
Models, Molecular
Molecular biophysics
Molecular Sequence Data
Peptides - chemistry
Protein Folding
Protein Structure, Secondary
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Summary:Design of functional foldamers requires knowledge of the conformational propensities of constituent residues. Here, we explore the effects of variations in both α-amino acid and β-amino acid substitution on α/β-peptide helicity. We also report the first X-ray crystal structure of a helical α/β-peptide. We conclude that a certain amount of conformational preorganization in α/β-peptides (via the inclusion of constrained β-amino acids or α,α-disubstituted α-amino acids) is needed to promote helical folding; acyclic β-amino acids and β-branched α-amino acids are tolerated to only a limited extent.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja0536163