The Source of Some of the Extraordinary Powers and Properties of Enzymes
Wiggins P1
1*Retired from the Department of Medicine, University of Auckland, New Zealand, and from Genesis Research and Development Company, Auckland, New Zealand.
Correspondence: p.wiggins@paradise.net.nz
Key Words: protein folding, water activity in solutions
Received 26 September 2008; revised 6 November 2008; accepted 5 January 2009. Published 1 July 2009. Available online 1 July 2009.
Summary
The generally successful model of liquid water, with its range of hydrogen bond strengths from weak to strong, fails to account for much of biochemistry. In particular it cannot supply the compensating decrease in free energy required to balance decreases in entropy in well-explored processes such as protein folding in solution. A simplified model in which there are just two strengths of hydrogen bonds seems to account as well for the broad bands of the vibrational spectrum of water, and at the same time has an inbuilt reservoir of free energy which can be harnessed to balance the decrease in entropy and increase of complexity of so many biochemical processes.