Pretransition-state protonation and the rate of chymotrypsin catalysis.
AUTOR(ES)
Wang, J H
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=223856Documentos Relacionados
- Protein hydration changes during catalysis: a new mechanism of enzymic rate-enhancement and ion activation/inhibition of catalysis.
- Visualization of intermediate and transition-state structures in protein-tyrosine phosphatase catalysis.
- Energetics of enzyme catalysis.
- Catalysis by acetylcholinesterase: evidence that the rate-limiting step for acylation with certain substrates precedes general acid-base catalysis.
- Plant pathogenic RNAs and RNA catalysis.