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.
|Number of pages||4|
|Journal||Biochemical and biophysical research communications|
|Publication status||Published - jún. 1 2007|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology