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Title: Movement and self-control in protein assemblies: quasi-equivalence revisited

Journal Article · · Biophys. J.; (United States)

Purposeful switching among different conformational states exerts self-control in the construction and action of protein assemblies. Quasi-equivalence, conceived to explain icosahedral virus structure, arises by differentiation of identical protein subunits into different conformations that conserve essential bonding specificity. Mechanical models designed to represent the energy distribution in the structure, rather than just the arrangement of matter, are used to explore flexibility and self-controlled movements in virus particles. Information about the assembly of bacterial flagella, actin, tobacco mosaic virus and the T4 from an inactive, unsociable form to an active, associable form. Energy to drive this change is provided by the intersubunit bonding in the growing structure; this self-control of assembly by conformational switching is called autostery, by homology with allostery. A mechanical model of the contractile T4 tail sheath has been constructed to demonstrate how self-controlled activation of latent bonding potential can drive a purposeful movement. The gradient of quasi-equivalent conformations modelled in the contracting tail sheath has suggested a workable mechanism for self-determination of tail tube length. Concerted action by assembles of identical proteins may often depend on individually differentiated movements.

Research Organization:
Brandeis Univ., Waltham, MA
OSTI ID:
6761379
Journal Information:
Biophys. J.; (United States), Vol. 32:1
Country of Publication:
United States
Language:
English