Helical folding in heterogeneous foldamers without inter-residual backbone hydrogen-bonding

This communication describes a set of hybrid foldamers that do not feature inter-residual, but intra-residual backbone hydrogen-bonding, yet adopt a preferentially folded conformation displaying right-handed helical architecture. Conformational ordering is apparently due to the combined conformation...

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Published inChemical communications (Cambridge, England) Vol. 48; no. 71; pp. 8922 - 8924
Main Authors Priya, Gowri, Kotmale, Amol S, Gawade, Rupesh L, Mishra, Deepti, Pal, Sourav, Puranik, Vedavadi G, Rajamohanan, Pattuparambil R, Sanjayan, Gangadhar J
Format Journal Article
LanguageEnglish
Published England 14.09.2012
Subjects
Amino Acids - chemistry
Carboxylic Acids - chemistry
Crystallography, X-Ray
Hydrogen - chemistry
Hydrogen Bonding
Peptides - chemistry
Peptides - metabolism
Protein Folding
Protein Structure, Secondary
Thiophenes - chemistry
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Summary:This communication describes a set of hybrid foldamers that do not feature inter-residual, but intra-residual backbone hydrogen-bonding, yet adopt a preferentially folded conformation displaying right-handed helical architecture. Conformational ordering is apparently due to the combined conformational restrictions imposed by the conformationally restricted individual amino acid residues with which the oligomers are made of.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1359-7345
1364-548X
DOI:10.1039/c2cc33235c