A model of myoglobin self-organization.
The self-organization of helical regions of myoglobin into a compact tertiary structure is considered on the basis of the hypothesis on the step-wise mechanism of self-organization of protein molecules. It is assumed that the self-organization begins with the formation of "centers of crystallization" and proceeds with the growth of on such center or by a sequential collapse of two or more grown centers. Different pathways of self-organization of myoglobin are considered; the most favourable structures corresponding to the greatest number of dehydrated bulky hydrophobic groups and to all the strongly hydrophilic groups exposed to water are selected at every stage of the given pathway and the others are neglected. One of the two most favourable structures obtained in such a way coincides in rough resolution with the native tertiary structure of protein.
D000818:Animals; D001665:Binding Sites; D008958:Models, Molecular; D009211:Myoglobin; D011485:Protein Binding; D011487:Protein Conformation; D014907:Whales
D009211:Myoglobin