Characterization of Asx Turn Types and Their Connate Relationship with β-Turns.

Autor: D'mello VC; Université Paris-Saclay, CEA, CNRS, Laboratoire Interactions Dynamiques et Lasers (LIDYL), 91191, Gif-sur-Yvette, France.; Present address: Graphene Research Labs, KIADB IT Park, Near Airport Bengaluru, 562149, India., Goldsztejn G; Université Paris-Saclay, CEA, CNRS, Laboratoire Interactions Dynamiques et Lasers (LIDYL), 91191, Gif-sur-Yvette, France.; Present address: Université Paris-Saclay, CNRS, Institut des Sciences Moléculaires d'Orsay (ISMO), 91405, Orsay, France., Rao Mundlapati V; Université Paris-Saclay, CEA, CNRS, Laboratoire Interactions Dynamiques et Lasers (LIDYL), 91191, Gif-sur-Yvette, France.; Present address: Institut de Recherche en Astrophysique et Planétologie (IRAP), Université de Toulouse (UPS), CNRS, CNES, 9 Avenue du Colonel Roche, 31028, Toulouse, France., Brenner V; Université Paris-Saclay, CEA, CNRS, Laboratoire Interactions Dynamiques et Lasers (LIDYL), 91191, Gif-sur-Yvette, France., Gloaguen E; Université Paris-Saclay, CEA, CNRS, Laboratoire Interactions Dynamiques et Lasers (LIDYL), 91191, Gif-sur-Yvette, France., Charnay-Pouget F; Université Paris-Saclay, CNRS, Institut de Chimie Moléculaire et des Matériaux d'Orsay (ICMMO), 91405, Orsay, France.; Present address: Université Clermont Auvergne, CNRS, SIGMA Clermont, ICCF, 63000, Clermont-Ferrand, France., Aitken DJ; Université Paris-Saclay, CNRS, Institut de Chimie Moléculaire et des Matériaux d'Orsay (ICMMO), 91405, Orsay, France., Mons M; Université Paris-Saclay, CEA, CNRS, Laboratoire Interactions Dynamiques et Lasers (LIDYL), 91191, Gif-sur-Yvette, France.
Jazyk: angličtina
Zdroj: Chemistry (Weinheim an der Bergstrasse, Germany) [Chemistry] 2022 May 02; Vol. 28 (25), pp. e202104328. Date of Electronic Publication: 2022 Mar 28.
DOI: 10.1002/chem.202104328
Abstrakt: Models of asparagine-containing dipeptides specifically designed to favor intrinsic folding into an Asx turn were characterized both theoretically, by using quantum chemistry, and experimentally, by using laser spectroscopy in the gas phase. Both approaches provided evidence for the spontaneous folding of both the Asn-Ala and Asn-Gly dipeptide models into the most stable Asx turn, a conformation stabilized by a C10 H-bond that was very similar to a type II' β-turn. In parallel, analysis of Asx turns implicating asparagine in crystallized protein structures in the Protein Data Bank revealed a sequence-dependent behavior. In Asn-Ala sequences, the Asx turn was found in conjunction with a type I β-turn for which the first of the four defining residues was Asn. The observation that the Asx turn in these structures is mostly of type II' (i. e., its most stable innate structure) suggests that this motif might foster the formation and/or enhance the stability of the backbone β-turn. In contrast, the Asx turns observed in Asn-Gly sequences extensively adopted a type II Asx-turn structure, thus suggesting that their formation should be ascribed to other factors, such as hydration. The fact that the Asx turn in a Asn-Gly sequence is also often found in combination with a hydrated β-bulge supports the premise that a Asn-Gly sequence might efficiently promote the formation of the β-bulge secondary structure.
(© 2022 Wiley-VCH GmbH.)
Databáze: MEDLINE
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