Reply to Karplus: Conformational dynamics have no role in the chemical step

Proceedings of the National Academy of Sciences of the United States of America

Volumn 107, Issue 17, 2010, Pages

  Kamerlin, Shina C L ^a   Warshel, Arieh ^a  

^a UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENYLATE KINASE;

CALIBRATION; CATALYSIS; CHEMICAL REACTION; CONFORMATION; ELECTRICITY; ENZYME ANALYSIS; LETTER; PRIORITY JOURNAL;

EID: 77952340641     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1002658107     Document Type: Letter

References (5)

1. Karplus M (2010) The role of conformation transitions in adenylate kinase. Proc Natl Acad Sci USA 107:E71.
2. Pisliakov AV, Cao J, Kamerlin SC, Warshel A (2009) Enzyme millisecond conformational dynamics do not catalyze the chemical step. Proc Natl Acad Sci USA 106:17359-17364.
3. Kamerlin SCL, Warshel A (2010) At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis? Proteins: Struct Func Bioinformat 78: 1339-1375.
4. Warshel A (1978) Energetics of enzyme catalysis. Proc Natl Acad Sci USA 75:5250-5254.
5. Warshel A, Parson WW (2001) Dynamics of biochemical and biophysical reactions: Insight from computer simulations. Q Rev Biophys 34:563-679. (Pubitemid 34127275)