Retention of Coiled-Coil Dimer Formation in the Absence of Ion Pairing at Positions Flanking the Hydrophobic Core

Hydrophobic interactions govern how proteins fold and interact with other molecules, but the impact of nearby polar functionality on the effective hydrophobicity of nonpolar surfaces remains unclear. Here we use a common protein quaternary structure motif, the parallel coiled-coil dimer, to ask whet...

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Veröffentlicht in:	Biochemistry (Easton) 2019-12, Vol.58 (48), p.4821-4826
Hauptverfasser:	Biok, Naomi A, Passow, Alexander D, Wang, Chenxuan, Bingman, Craig A, Abbott, Nicholas L, Gellman, Samuel H
Format:	Artikel
Sprache:	eng
Online-Zugang:	Volltext
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