Delineation of a new structural motif involving NHN γ-turn.
helix capping
hydrogen bonding
protein conformation
protein loops
structural motifs
γ-turn
Journal
Proteins
ISSN: 1097-0134
Titre abrégé: Proteins
Pays: United States
ID NLM: 8700181
Informations de publication
Date de publication:
03 2020
03 2020
Historique:
received:
16
04
2019
revised:
17
09
2019
accepted:
18
09
2019
pubmed:
7
10
2019
medline:
5
1
2021
entrez:
7
10
2019
Statut:
ppublish
Résumé
Macromolecules are characterized by distinctive arrangement of hydrogen bonds. Different patterns of hydrogen bonds give rise to distinct and stable structural motifs. An analysis of 4114 non-redundant protein chains reveals the existence of a three-residue, (i - 1) to (i + 1), structural motif, having two hydrogen-bonded five-membered pseudo rings (the first, an NH···OC involving the first residue, and the second being NH∙∙∙N involving the last two residues), separated by a peptide bond. There could be an additional hydrogen bond between the side-chain at (i-1) and the main-chain NH of (i + 1). The average backbone torsion angles of -76(±21)° and - 12(±17)° at i creates a tight turn in the polypeptide chain, akin to a γ-turn. Indeed, a search of three-residue fragments with restriction on the terminal C
Substances chimiques
Amino Acids
0
Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
431-439Informations de copyright
© 2019 Wiley Periodicals, Inc.
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