Title : Hydrolysis of cyclic phosphates by ribonuclease A: a computational study using a simplified ab initio quantum model.

Pub. Date : 2003 Nov 15

PMID : 12964199






4 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 The second step in the enzyme-catalyzed hydrolysis of phosphate esters by ribonuclease A (RNase A) was studied using an ab initio quantum-based model of the active site including constrained parts of three critical residues, His-12, His-119, and Lys-41, and a small substrate. Histidine ribonuclease A family member 1, pancreatic Homo sapiens
2 The second step in the enzyme-catalyzed hydrolysis of phosphate esters by ribonuclease A (RNase A) was studied using an ab initio quantum-based model of the active site including constrained parts of three critical residues, His-12, His-119, and Lys-41, and a small substrate. Histidine ribonuclease A family member 1, pancreatic Homo sapiens
3 The second step in the enzyme-catalyzed hydrolysis of phosphate esters by ribonuclease A (RNase A) was studied using an ab initio quantum-based model of the active site including constrained parts of three critical residues, His-12, His-119, and Lys-41, and a small substrate. Histidine ribonuclease A family member 1, pancreatic Homo sapiens
4 The second step in the enzyme-catalyzed hydrolysis of phosphate esters by ribonuclease A (RNase A) was studied using an ab initio quantum-based model of the active site including constrained parts of three critical residues, His-12, His-119, and Lys-41, and a small substrate. Histidine ribonuclease A family member 1, pancreatic Homo sapiens