C.N. Jones

Works (1)

Updated: July 5th, 2023 15:48

2010 article

Kinetic Stability May Determine the Interaction Dynamics of the Bifunctional Protein DCoH1, the Dimerization Cofactor of the Transcription Factor HNF-1α,

Rho, H., Jones, C. N., & Rose, R. B. (2010, October 26). Biochemistry, Vol. 49, pp. 10187–10197.

By: H. Rho n, C. Jones n & R. Rose n 

MeSH headings : Chromatography, Gel; Enzyme Stability; Guanidine / pharmacology; Hepatocyte Nuclear Factor 1-alpha / metabolism; Hydro-Lyases / genetics; Hydro-Lyases / metabolism; Kinetics; Models, Molecular; Point Mutation; Protein Denaturation; Protein Multimerization; Protein Unfolding; Spectrometry, Fluorescence; Tryptophan / chemistry
topics (OpenAlex): Pancreatic function and diabetes; Diet, Metabolism, and Disease; Enzyme Structure and Function
TL;DR: This work shows that a point mutation at the DCoH1 tetramer interface, Thr 51 Ser, overcomes the dissociation barrier of the homotetramer and increases the interaction with HNF-1α, and proposes an unfolding pathway in which the tetramer unfolds slowly, but the dimer folds reversibly. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

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