Atomic scale determination of enzyme flexibility and active site stability through static modes: case of dihydrofolate reductase.

Brut, Marie; Estève, Alain; Landa, Georges; Renvez, Guillaume; Djafari Rouhani, Mehdi; Vaisset, Marc

Brut, Marie; Estève, Alain; Landa, Georges; Renvez, Guillaume; Djafari Rouhani, Mehdi; Vaisset, Marc.

Affiliation

Brut M; LAAS-CNRS, Université de Toulouse, 7 avenue du Colonel Roche, F-31077 Toulouse, France. mbrut@stanford.edu

J Phys Chem B ; 115(7): 1616-22, 2011 Feb 24.

Article in En | MEDLINE | ID: mdl-21287995

Subject(s)

Tetrahydrofolate Dehydrogenase/chemistry; Catalytic Domain; Enzyme Stability; Escherichia coli/enzymology; Protein Conformation; Tetrahydrofolate Dehydrogenase/metabolism

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Tetrahydrofolate Dehydrogenase Language: En Journal: J Phys Chem B Journal subject: QUIMICA Year: 2011 Document type: Article Affiliation country: France Country of publication: United States

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