Switching an active site helix in dihydrofolate reductase reveals limits to subdomain modularity.

Zhao, Victor Y; Rodrigues, João V; Lozovsky, Elena R; Hartl, Daniel L; Shakhnovich, Eugene I

Zhao, Victor Y; Rodrigues, João V; Lozovsky, Elena R; Hartl, Daniel L; Shakhnovich, Eugene I.

Afiliación

Zhao VY; Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts.
Rodrigues JV; Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts.
Lozovsky ER; Department of Organismic and Evolutionary Biology, Harvard University, Cambridge, Massachusetts.
Hartl DL; Department of Organismic and Evolutionary Biology, Harvard University, Cambridge, Massachusetts.
Shakhnovich EI; Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts. Electronic address: shakhnovich@chemistry.harvard.edu.

Biophys J ; 120(21): 4738-4750, 2021 11 02.

Article en En | MEDLINE | ID: mdl-34571014

Asunto(s)

Escherichia coli; Tetrahidrofolato Deshidrogenasa; Dominio Catalítico; Escherichia coli/genética; Escherichia coli/metabolismo; Cinética; Conformación Proteica; Tetrahidrofolato Deshidrogenasa/genética

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Contexto en salud: 3_ND Problema de salud: 3_neglected_diseases / 3_zoonosis Asunto principal: Tetrahidrofolato Deshidrogenasa / Escherichia coli Tipo de estudio: Prognostic_studies Idioma: En Revista: Biophys J Año: 2021 Tipo del documento: Article

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