Conformational Preferences of Short Peptide Fragments

Conformational Preferences of Short Peptide Fragments

Folding in the confine: Short fragments of tri‐ to hexapeptides have been encapsulated by a synthetic host in water and folded into their latent helical structures (see crystal structure). Crystallographic analysis of the complexes clearly reveals a mixed conformation of 310 and α helices, thereby i...

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Veröffentlicht in:Angewandte Chemie (International ed.) 2009-11, Vol.48 (46), p.8695-8698
Hauptverfasser: Hatakeyama, Yoshiyuki, Sawada, Tomohisa, Kawano, Masaki, Fujita, Makoto
Format: Artikel
Sprache:eng
Schlagworte:
Crystallography, X-Ray
helical structures
host-guest systems
Hydrophobic and Hydrophilic Interactions
Molecular Conformation
Peptide Fragments - chemistry
peptides
self-assembly
structure elucidation
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container_end_page 8698
container_issue 46
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container_title Angewandte Chemie (International ed.)
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creator Hatakeyama, Yoshiyuki
Sawada, Tomohisa
Kawano, Masaki
Fujita, Makoto
description Folding in the confine: Short fragments of tri‐ to hexapeptides have been encapsulated by a synthetic host in water and folded into their latent helical structures (see crystal structure). Crystallographic analysis of the complexes clearly reveals a mixed conformation of 310 and α helices, thereby illustrating the inherent helical propensity of very short peptide fragments.
doi_str_mv 10.1002/anie.200903563
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subjects Crystallography, X-Ray
helical structures
host-guest systems
Hydrophobic and Hydrophilic Interactions
Molecular Conformation
Peptide Fragments - chemistry
peptides
self-assembly
structure elucidation
title Conformational Preferences of Short Peptide Fragments
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