Hydrogen exchange of chemoreceptors in functional complexes suggests protein stabilization mediates long-range allosteric coupling.

Li, Xuni; Eyles, Stephen J; Thompson, Lynmarie K

Li, Xuni; Eyles, Stephen J; Thompson, Lynmarie K.

Affiliation

Li X; Department of Chemistry, University of Massachusetts Amherst, Amherst, Massachusetts 01003.
Eyles SJ; Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, Massachusetts 01003.
Thompson LK; Department of Chemistry, University of Massachusetts Amherst, Amherst, Massachusetts 01003 thompson@chem.umass.edu.

J Biol Chem ; 294(44): 16062-16079, 2019 11 01.

Article in En | MEDLINE | ID: mdl-31506298

Subject(s)

Allosteric Site; Escherichia coli Proteins/chemistry; Histidine Kinase/chemistry; Methyl-Accepting Chemotaxis Proteins/chemistry; Allosteric Regulation; Deuterium Exchange Measurement; Escherichia coli Proteins/metabolism; Histidine Kinase/metabolism; Liposomes/chemistry; Methyl-Accepting Chemotaxis Proteins/metabolism; Protein Stability; Signal Transduction

Key words

allosteric regulation; bacterial signal transduction; chemoreceptor; chemotaxis; hydrogen-deuterium exchange; intrinsically disordered protein; membrane protein; protein complex; receptor structure-function; transmembrane signaling

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Escherichia coli Proteins / Allosteric Site / Histidine Kinase / Methyl-Accepting Chemotaxis Proteins Language: En Journal: J Biol Chem Year: 2019 Document type: Article Country of publication: United States

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