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Peptide beta-Bend and 3(10)-Helix: from 3D-Structural Studies to Applications as Templates.

Academic Article
Publication Date:
2005
abstract:
The 3(10)-helix is a relatively common secondary structure motif in peptides and proteins. Its building block is one of various types of beta-bend conformation which comprises an N(alpha)-acylated dipeptide alkylamide system. A complete 3D-structural characterization of this ternary helix has been achieved, thus allowing its unambiguous discrimination from the closely related a-helix. Recent applications of rigidified peptide beta-bends and 3(10)-helices as templates for investigations in synthetic organic chemistry (macrocyclization, catalysis), host-guest chemistry (molecular recognition), and physical chemistry (donor-acceptor interaction) will be discussed.
Iris type:
01.01 Articolo in rivista
List of contributors:
Crisma, Marco
Handle:
https://iris.cnr.it/handle/20.500.14243/164976
Published in:
JOURNAL OF INCLUSION PHENOMENA AND MOLECULAR RECOGNITION IN CHEMISTRY
Journal
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