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Physical properties of capsids of plant and animal viruses are importantfactors in capsid self-assembly, survival of viruses in the extracellularenvironment, and their cell infectivity. Virus shells can have applications asnanocontainers and delivery vehicles in biotechnology and medicine. CombinedAFM experiments and computational modeling on sub-second timescales of theindentation nanomechanics of Cowpea Chlorotic Mottle Virus (CCMV) capsid showthat the capsid's physical properties are dynamic and local characteristics ofthe structure, which depend on the magnitude and geometry of mechanical input.Surprisingly, under large deformations the CCMV capsid transitions to thecollapsed state without substantial local structural alterations. The enthalpychange in this deformation state dH = 11.5 - 12.8 MJ/mol is mostly due tolarge-amplitude out-of-plane excitations, which contribute to the capsidbending, and the entropy change TdS = 5.1 - 5.8 MJ/mol is mostly due tocoherent in-plane rearrangements of protein chains, which result in the capsidstiffening. Dynamic coupling of these modes defines the extent of elasticityand reversibility of capsid mechanical deformation. This emerging pictureilluminates how unique physico-chemical properties of protein nanoshells helpdefine their structure and morphology, and determine their viruses' biologicalfunction.

Structural transitions and energy landscape for Cowpea Chlorotic Mottle Virus capsid mechanics from nanomanipulation in vitro and in silico