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

Chapter 2: Quasi-Equivalence and Adaptability in Living Molecular Assemblies

Donald L. Caspar,
Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306-4380.
Email address: Caspar@fsu.edu
Lena Hammar,
Department of Biosciences, Korolinska Institute, Stockholm Sweden.
Email address: lena.hammar@biosci.ki.se

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.

INTRODUCTION

Knowledge is the astonishing consequence of mans shortcomings; it has evolved from confusion, errors and chaos. But, as put by Francis Bacon, truth emerges more easily from error than from confusion. Therefore, for making any progress with confusing and complicated problems, some simple rules are very helpful, also if they will be proven wrong! Discoveries and theories very often turn out to be wrong regarding the phenomenon they were developed for. Nevertheless, they may be right in some other aspects! Searched and utilized with an open mind, theorems could make life...

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