Cheung, EY and McCabe, EE and Harris, KDM and Johnston, RL and Tedesco, E and Raja, KMP and Balaram, P (2002) C-H center dot center dot center dot O hydrogen bond mediated chain reversal in a peptide containing a \gamma-amino acid residue, determined directly from powder X-ray diffraction data. In: Wiley-Vch Verlag GmbH, 41 (3). pp. 494-496.
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The finding that peptides containing -amino acid residues give rise to folding patterns hitherto unobserved in -amino acid peptides has stimulated considerable interest in the conformational properties of peptides built from , , and residues, as the introduction of additional methylene (CH2) units into peptide chains provides further degrees of conformational freedom. Studies of the influence of introducing-amino acids into regular polypeptide structures derived from residues have demonstrated that extra methylene groups can be inserted into helical backbones and into the strand and turn segments of hairpins. In regard to the influence of CH2 group insertion into the i2 position of isolated peptide turns, we are investigating the conformational properties of a series of model sequences Piv-Pro-Xxx- NHMe (defined in Scheme 1 and reference ).
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Wiley-Vch Verlag GmbH.|
|Keywords:||Crystal-Structure Determination;Genetic Algorithm;Secondary Structure;Beta-Peptides;Design;Conformations;Hexapeptide; Patterns;Proteins;Helices|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||09 Mar 2009 11:48|
|Last Modified:||19 Sep 2010 05:00|
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