Richard JP

Uncovering the Role of Key Active-Site Side Chains in Catalysis: An Extended Brønsted Relationship for Substrate Deprotonation Catalyzed by Wild-Type and Variants of Triosephosphate Isomerase.

Kulkarni YS, Amyes TL, Richard JP, Kamerlin SCL

Journal of the American Chemical Society 141 (40) 16139-16150 [2019-10-09; online 2019-09-25]

Uncovering the Role of Key Active Site Side Chains in Catalysis: An Extended Brønsted Relationship for Substrate Deprotonation Catalysed by Wild-Type and Variants of Triosephosphate Isomerase

Kulkarni YS, Amyes TL, Richard J, Kamerlin SCL

- - (-) - [2019-08-13; online 2019-08-13]

Human Glycerol 3-Phosphate Dehydrogenase: X-ray Crystal Structures That Guide the Interpretation of Mutagenesis Studies.

Mydy LS, Cristobal JR, Katigbak RD, ..., Richard JP, Gulick AM

Biochemistry 58 (8) 1061-1073 [2019-02-26; online 2019-01-31]

Role of Ligand-Driven Conformational Changes in Enzyme Catalysis: Modeling the Reactivity of the Catalytic Cage of Triosephosphate Isomerase.

Kulkarni YS, Liao Q, Byléhn F, ..., Richard JP, Kamerlin SCL

Journal of the American Chemical Society 140 (11) 3854-3857 [2018-03-21; online 2018-03-13]

Enzyme Architecture: Modeling the Operation of a Hydrophobic Clamp in Catalysis by Triosephosphate Isomerase.

Kulkarni YS, Liao Q, Petrović D, ..., Richard JP, Kamerlin SCL

Journal of the American Chemical Society 139 (30) 10514-10525 [2017-08-02; online 2017-07-19]