Protein self-association in the cell: a mechanism for fine tuning the level of macromolecular crowding?
A new role for protein self-association in the cell is discussed. An argument is advanced that when cellular protein is in its associated state the excluded volume component of the solution is minimized. Conversely, when cellular protein is in its dissociated state the excluded volume component of the solution is maximized. For proteins that make up a substantial fraction of the intracellular protein concentration, control of the self-association event thus presents itself as a means of regulating cellular processes that are influenced by different levels of volume exclusion. In this communication we examine how the control of protein association/dissociation might influence one such important process, namely the folding of a protein to a compact state.
Hall
Damien
D
Chemistry Department, University of Cambridge, Lensfield Road, Cambridge, CB21EW, UK. drh32@cam.ac.uk
D003198:Computer Simulation; D042541:Intracellular Space / Q000737:chemistry / Q000648:ultrastructure; D046911:Macromolecular Substances / Q000737:chemistry; D008962:Models, Theoretical; D010316:Particle Size; D017510:Protein Folding; D013816:Thermodynamics
D046911:Macromolecular Substances