Quantitatively probing propensity for structural transitions in engineered virus nanoparticles by single-molecule mechanical analysis.
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Structural basis for biologically relevant mechanical stiffening of a virus capsid by cavity-creating or spacefilling mutations.Structural Analysis of a Temperature-Induced Transition in a Viral Capsid Probed by HDX-MS.Kinetics of Surface-Driven Self-Assembly and Fatigue-Induced Disassembly of a Virus-Based Nanocoating.Assembly, Engineering and Applications of Virus-Based Protein Nanoparticles.Quantification and modification of the equilibrium dynamics and mechanics of a viral capsid lattice self-assembled as a protein nanocoating.Systematic analysis of biological roles of charged amino acid residues located throughout the structured inner wall of a virus capsid.
P2860
Quantitatively probing propensity for structural transitions in engineered virus nanoparticles by single-molecule mechanical analysis.
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@zh-hk
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name
Quantitatively probing propens ...... -molecule mechanical analysis.
@en
type
label
Quantitatively probing propens ...... -molecule mechanical analysis.
@en
prefLabel
Quantitatively probing propens ...... -molecule mechanical analysis.
@en
P2093
P2860
P356
P1433
P1476
Quantitatively probing propens ...... -molecule mechanical analysis.
@en
P2093
Mauricio G Mateu
Milagros Castellanos
Pablo J P Carrillo
P2860
P304
P356
10.1039/C4NR07046A
P407
P577
2015-03-01T00:00:00Z