Controlling crystallization and its absence: proteins, colloids and patchy models.
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.
Doye
Jonathan P K
JP
Physical and Theoretical Chemistry Laboratory, Oxford University, South Parks Road, Oxford, UK OX1 3QZ. jonathan.doye@chem.ox.ac.uk
Louis
Ard A
AA
Lin
I-Chun
IC
Allen
Lucy R
LR
Noya
Eva G
EG
Wilber
Alex W
AW
Kok
Hoong Chwan
HC
Lyus
Rosie
R
D003102:Colloids / Q000737:chemistry*; D003198:Computer Simulation; D003460:Crystallization; D007700:Kinetics; D008956:Models, Chemical; D011506:Proteins / Q000737:chemistry*
D003102:Colloids; D011506:Proteins