Effects of single nucleotide polymorphisms on human N-acetyltransferase 2 structure and dynamics by molecular dynamics simulation

Medicine & Life Sciences

• human NAT2 protein 100%
• Acetyltransferases 64%
• Molecular Dynamics Simulation 55%
• Single Nucleotide Polymorphism 41%
• Static Electricity 39%
• Binding Sites 38%
• Mutation 28%
• Arylamine N-Acetyltransferase 27%
• hydrazine 24%
• Proteins 18%
• Enzymes 18%
• Amino Acid Substitution 18%
• Drug-Related Side Effects and Adverse Reactions 15%
• Pharmaceutical Preparations 6%
• Population 6%
• Neoplasms 5%

Agriculture & Biology

• molecular dynamics 63%
• acetyltransferases 61%
• single nucleotide polymorphism 46%
• binding sites 31%
• mutants 29%
• catalytic activity 23%
• arylamine N-acetyltransferase 21%
• genetic polymorphism 18%
• drug toxicity 17%
• mutation 17%
• hydrazine 16%
• induced mutation 15%
• human population 13%
• amino acid substitution 13%
• protein structure 12%
• enzymes 11%
• neoplasms 9%
• proteins 8%
• drugs 8%
• methodology 3%

Chemistry

• Cofactor 45%
• Mutation 42%
• Nucleotide 41%
• Molecular Dynamics 36%
• Binding Site 35%
• Electrostatic Potential 34%
• Carcinogenic 17%
• Drug 17%
• Protein Structure 16%
• Hydrazine 15%
• Protein 13%
• Shape 10%
• Substitution Reaction 10%
• Acid 5%