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Handedness preference and switching of peptide helices. Part II: Helices based on noncoded alpha-amino acids

Academic Article
Publication Date:
2015
abstract:
In this second part of our review article on the preferred screw sense and interconversion of peptide helices, we discuss the most significant computational and experimental data published on helices formed by the most extensively investigated categories of noncoded alpha-amino acids. They are as follows: (i) N-alkylated Gly residues (peptoids), (ii) C-alkylated alpha-amino acids, (iii) C-alpha,C-beta-sp(2) configurated alpha-amino acids, and (iv) combinations of residues of types (ii) and (iii). With confidence, the large body of interesting papers examined and classified in this editorial effort will stimulate the development of helical peptides in many diverse areas of biosciences and nanosciences. Copyright (c) 2015 European Peptide Society and John Wiley & Sons, Ltd.
Iris type:
01.01 Articolo in rivista
Keywords:
chirality; handedness; helical structures; nuclear magnetic resonance; peptides; X-ray diffraction crystallography; spectroscopy; switches
List of contributors:
Formaggio, Fernando; Toniolo, Claudio; Moretto, Alessandro; Crisma, Marco
Handle:
https://iris.cnr.it/handle/20.500.14243/296557
Published in:
JOURNAL OF PEPTIDE SCIENCE (PRINT)
Journal
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