Solid-State <sup>17</sup>O NMR of Unstable Acyl-Enzyme Intermediates: A Direct Probe of Hydrogen Bonding Interactions in the Oxyanion Hole of Serine Proteases.

Tang, Aaron W; Kong, Xianqi; Terskikh, Victor; Wu, Gang

Solid-State ¹⁷O NMR of Unstable Acyl-Enzyme Intermediates: A Direct Probe of Hydrogen Bonding Interactions in the Oxyanion Hole of Serine Proteases.

Tang, Aaron W; Kong, Xianqi; Terskikh, Victor; Wu, Gang.

Afiliación

Tang AW; Department of Chemistry, Queen's University , 90 Bader Lane, Kingston, Ontario K7L 3N6, Canada.
Kong X; Department of Chemistry, Queen's University , 90 Bader Lane, Kingston, Ontario K7L 3N6, Canada.
Terskikh V; Department of Chemistry, Queen's University , 90 Bader Lane, Kingston, Ontario K7L 3N6, Canada.
Wu G; Department of Chemistry, University of Ottawa , Ottawa, Ontario K1N 6N5, Canada.

J Phys Chem B ; 120(43): 11142-11150, 2016 11 03.

Article en En | MEDLINE | ID: mdl-27731644

Asunto(s)

Quimotripsina/química; Resonancia Magnética Nuclear Biomolecular; Oxígeno/química; Serina Proteasas/química; Aniones/química; Quimotripsina/metabolismo; Enlace de Hidrógeno; Estructura Molecular; Isótopos de Oxígeno; Serina Proteasas/metabolismo

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Bases de datos: MEDLINE Asunto principal: Oxígeno / Quimotripsina / Resonancia Magnética Nuclear Biomolecular / Serina Proteasas Idioma: En Revista: J Phys Chem B Asunto de la revista: QUIMICA Año: 2016 Tipo del documento: Article País de afiliación: Canadá

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