Conformational Proteomics of Macromolecular Architecture: Approaching the Structure of Large Molecular Assemblies and their Mechanisms of Action

The quest for relations between form and function is the substance of structural molecular biology. Biological systems combine a high degree of organization with a capacity for dynamic behavior. These features seem to originate from the specific bonding properties of protein molecules that can appear in more than one structural configuration. An attempt to explain how multiple copies of a protein can self-assemble into a cage with a strict symmetry lattice was given in the 1962 theory of quasi-equivalence. The same concept of protein adaptability may be used to approach dynamic behavior of regular biological assemblies as a general. We here describe the principle with two examples that did not originally apply to the theory.
Keywords: Virus architecture, spherical shell lattice, quasi-equivalent environment, tensegrity structure, 5-fold- and icosahedral symmetry.
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