Abstract
Bridging the gap between crystallized proteins and gas-phase models sheds light on the structure and the function of Asx turns. A comparison of the isolated Asx turns, based on an asparagine residue, observed in model peptides by using laser spectroscopic and quantum chemistry diagnostics, with the structures of crystallized proteins supports the premise that Asx turns foster or stabilize classical β-turn structures, and even promote β-bulges when Asn is followed by a Gly residue. More information can be found in the Research Article by D. J. Aitken, M. Mons et al. (DOI: 10.1002/chem.202104328).
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