Pages that link to "Q35108348"
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The following pages link to Understanding the Role of Active‐Site Residues in Chorismate Mutase Catalysis from Molecular‐Dynamics Simulations (Q35108348):
Displaying 14 items.
- How enzymes work: analysis by modern rate theory and computer simulations (Q28238088) (← links)
- Transition-State Charge Stabilization through Multiple Non-covalent Interactions in the Guanidinium-Catalyzed Enantioselective Claisen Rearrangement (Q34169712) (← links)
- The proficiency of a thermophilic chorismate mutase enzyme is solely through an entropic advantage in the enzyme reaction (Q34234772) (← links)
- The near attack conformation approach to the study of the chorismate to prephenate reaction (Q34267037) (← links)
- Deciphering enzymes. Genetic selection as a probe of structure and mechanism (Q35750741) (← links)
- Mechanisms and free energies of enzymatic reactions (Q35768462) (← links)
- How an enzyme surmounts the activation energy barrier (Q36347286) (← links)
- Preliminary X-ray crystallographic analysis of the secreted chorismate mutase from Mycobacterium tuberculosis: a tricky crystallization problem solved. (Q36417398) (← links)
- Quantum chemical modeling of the reaction path of chorismate mutase based on the experimental substrate/product complex (Q42027813) (← links)
- Conformational effects in enzyme catalysis: QM/MM free energy calculation of the 'NAC' contribution in chorismate mutase (Q44891391) (← links)
- Probing protein environment in an enzymatic process: All-electron quantum chemical analysis combined with ab initio quantum mechanical/molecular mechanical modeling of chorismate mutase (Q46221671) (← links)
- The catalytic power of enzymes: conformational selection or transition state stabilization? (Q51943696) (← links)
- QM/MM-Methoden für biomolekulare Systeme (Q57971613) (← links)
- Crystal structure of chorismate mutase from Burkholderia phymatum (Q61918865) (← links)