Theory of conformational transitions of viral shells.
We propose a continuum theory for the conformational transitions of viral shells. Conformational transitions of viral shells, as encountered during viral maturation, are associated with a soft mode instability of the capsid proteins [F. Tama and C. L. Brooks, J. Mol. Biol. 345(2), 299 (2005)]. The continuum theory presented here is an adaptation of the Ginzburg-Landau theory of soft-mode structural phase transitions of solids to viral shells. The theory predicts that the conformational transitions are characterized by a pronounced softening of the shell elasticity in the critical region. We demonstrate that the thermodynamics of the conformational transition can be probed quantitatively by a micromechanical atomic force microscope study. The external force can drive a capsid into a state of phase coexistence characterized by a highly nonlinear force deformation curve.
Guérin
Thomas
T
Ecole Polytechnique, 91128 Palaiseau, France.
Bruinsma
Robijn
R
D001703:Biophysics / Q000379:methods; D036022:Capsid Proteins / Q000737:chemistry; D018625:Microscopy, Atomic Force; D015233:Models, Statistical; D008968:Molecular Conformation; D009995:Osmosis; D011506:Proteins / Q000737:chemistry; D013314:Stress, Mechanical; D013816:Thermodynamics; D019065:Virus Assembly; D014780:Viruses / Q000378:metabolism*
D036022:Capsid Proteins; D011506:Proteins