โ Scribed by D. L. D. Caspar
No coin nor oath required. For personal study only.
Assemblies of protein molecules represent a fundamental level of biological organization. The dynamic behavior of these systemsincluding both the assembly process and functional rearrangementsmay be accounted for by the specificity of the protein interactions, which depend on environmental conditions. Analysis of the self-assembly of virus particles has established that the design of an ordered structure can be built into the specific bonding properties of the constituent proteins. Any structure which can change its state of organization is, by definition, polymorphic. The distinctive aspect of polymorphism in protein structures, contrasted with nonliving states of matter, is that the molecular design has been selected to carry out a function and that this function is part of an integrated system. The differences in molecular conformation and arrangement in all polymorphic structuresfor example, allosteric enzymes or ice crystalsdepend on the intrinsic interaction properties of the molecules themselves. The structures of ice and water illustrate relations between specificity and polymorphism which are relevant to the form and function of protein assemblies.
Two types of polymorphism can be distinguished: modal polymorphism, which is
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## Abstract New frontiers in materials and polymer science include the development of assembly processes that are flexible, allow the access and implementation of nanoscale structure and order, can provide access to a broad range of materials systems, and yet can be implemented at relatively low co