An Anion-π Interaction Strongly Stabilizes the β-Sheet Protein WW.

Autor:	Smith MS; Department of Chemistry and Biochemistry, Brigham Young University , Provo, Utah 84602, United States., Lawrence EEK; Department of Chemistry and Biochemistry, Brigham Young University , Provo, Utah 84602, United States., Billings WM; Department of Chemistry and Biochemistry, Brigham Young University , Provo, Utah 84602, United States., Larsen KS; Department of Chemistry and Biochemistry, Brigham Young University , Provo, Utah 84602, United States., Bécar NA; Department of Chemistry and Biochemistry, Brigham Young University , Provo, Utah 84602, United States., Price JL; Department of Chemistry and Biochemistry, Brigham Young University , Provo, Utah 84602, United States.
Jazyk:	angličtina
Zdroj:	ACS chemical biology [ACS Chem Biol] 2017 Oct 20; Vol. 12 (10), pp. 2535-2537. Date of Electronic Publication: 2017 Sep 14.
DOI:	10.1021/acschembio.7b00768
Abstrakt:	Anions have long been known to engage in stabilizing interactions with electron-deficient arenes. However, the precise nature and energetic contribution of anion-π interactions to protein stability remains a subject of debate. Here, we show that placing a negatively charged Asp in close proximity to electron-rich Phe in a reverse turn within the WW domain results in a favorable interaction that increases WW conformational stability by -1.3 kcal/mol.
Databáze:	MEDLINE
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