Structural and thermodynamic analyses of the β-to-α transformation in RfaH reveal principles of fold-switching proteins
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DOI: 10.1101/2022.01.14.476317
Abstract: The two-domain protein RfaH, a paralog of the universally conserved NusG/Spt5 transcription factors, is regulated by autoinhibition coupled to the reversible conformational switch of its 60-residue C-terminal KOW domain between an α-hairpin and a β-barrel.… read more here.
Keywords: kow; analyses transformation; thermodynamic analyses; nusg spt5 ... See more keywords