2007/01/01 by Jonathan P. K. Doye, Ard A. Louis, I-Chun Lin +5 · 200 citations
Materials Science · Physics and Astronomy · #Anisotropy #Biomolecule #Colloid #Colloidal particle #Crystallization #Enzyme Structure and Function #Globular protein #Material Dynamics and Properties #Metal #Pickering emulsions and particle stabilization #cond-mat.soft #cond-mat.stat-mech
paper · pdf · doi:10.1039/b614955c
published in Physical Chemistry Chemical Physics 9(18), 2197 (Royal Society of Chemistry) · 11 pages, 7 figures
openalex publication_date 2007/01/01 · arxiv created 2007/01/04 · openalex created_date 2016/06/24 · arxiv updated 2017/09/13 · openalex updated_date 2026/08/05
The ability to control the crystallization behaviour (including its absence) of particles, be they biomolecules such as globular proteins, inorganic colloids, nanoparticles, or metal atoms in an alloy, is of both fundamental and technological importance. Much can be learnt from the exquisite control that biological systems exert over the behaviour of proteins, where protein crystallization and aggregation are generally suppressed, but where in particular instances complex crystalline assemblies can be formed that have a functional purpose. We also explore the insights that can be obtained from computational modelling, focussing on the subtle interplay between the interparticle interactions, the preferred local order and the resulting crystallization kinetics. In particular, we highlight the role played by "frustration", where there is an incompatibility between the preferred local order and the global crystalline order, using examples from atomic glass formers and model anisotropic particles.