Gradionation: hypothesis for positioning and patterning.
The interaction of contiguous proteins is explored in microtubules, rosettes, and membranes based on the well established molecular phenomena of cooperativity and allosterism. It is proposed that conformational gradients in protein arrays cause the formation of gradions by nearest-neighbor interactions. Gradions are repeating functional molecular sequences that contain several conformational forms of one or more proteins, with the result that different reactive sites can exist in the same molecular architecture at any one time. Gradionators are small controlling molecules that may be microscopically visible as layers of linkages, but could alse be smaller. Some of the presently available supporting evidence and its functional implications are discussed, including the possibility that the raison d'etre for membrane-particle arrays is to enhance the regulation and amplification capabilities of cell systems.
D000494:Allosteric Regulation; D000818:Animals; D004798:Enzymes / Q000378:metabolism; D056890:Eukaryota / Q000378:metabolism / Q000648:ultrastructure; D008565:Membrane Proteins / Q000378:metabolism; D008566:Membranes / Q000648:ultrastructure; D008870:Microtubules / Q000648:ultrastructure; D008954:Models, Biological; D011487:Protein Conformation; D011506:Proteins / Q000378:metabolism; D014404:Tubulin / Q000378:metabolism
D004798:Enzymes; D008565:Membrane Proteins; D011506:Proteins; D014404:Tubulin