Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1937597 | Biochemical and Biophysical Research Communications | 2007 | 4 Pages |
Abstract
The functioning of enzymes and protein folding are well known to be assisted by the surrounding chaperoning water molecules, which are connected to the protein via non-covalent, dynamically changing chemical bonds. A molecular intracellular network of weak non-covalent connections may be presumed to exist in living cells. The roles of such non-covalent networks are examined in terms of a molecular model which postulates a universal enzyme and biochemical mechanism regulating the maintenance of chemical stability in living cells.
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Authors
Zoltán Szolnoki,