In spite of current concepts, it appears to be surface water which, by moving from randomness toward cubic order on surfaces and then back to randomness, that drives polypeptides toward order. Insulin is a good example.
The Order/Disorder properties of water appear to play a critical role in the catalytic hydrolyses of aromatic peptides from the ends of polypeptide chains. Here is a graphic interpretation of that role.
Ribonuclease A is presented below as an example of how surface water, by repetitively forming picosecond cubic ice linear elements of hydration on lipid and poly-ionic surfaces of its polypeptide, not only assists in directing and driving its wrapping and assembly into its protein structure, but its enzymatic properties as well.
The article describes how transient linear elements of surface hydration most likely assist in directing and driving the folding and assembly of the polypeptide of alpha chymotrypsin into the active enzyme and how it assists in catalytic cleavage of polypeptides.
Ubiquitins are a family of proteins which bind to other proteins and carry them to digestive enzymes which return them to the aninoacids. They are the cleaning-ladies of the cell.
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