The impact of conformational fluctuations on self-assembly: cooperative aggregation of archaeal chaperonin proteins.
Protein complexes called rosettasomes self-assemble in solution to form large-scale filamentous and planar structures. The relative abundance of these aggregates varies abruptly with environmental conditions and sample composition. Our simulations of a model of patchy nanoparticles can reproduce this sharp crossover, but only if particles are allowed to switch between two internal states favoring different geometries of local binding. These results demonstrate how local conformational adaptivity can fundamentally influence the cooperativity of pattern-forming dynamics.
Whitelam
Stephen
S
Systems Biology Centre, University of Warwick, Coventry CV4 7AL, U.K., Biophysics Graduate Group, University of California at Berkeley, Berkeley, California 94720, USA.
Rogers
Carl
C
Pasqua
Andrea
A
Paavola
Chad
C
Trent
Jonathan
J
Geissler
Phillip L
PL
D018833:Chaperonins / Q000737:chemistry* / Q000648:ultrastructure*; D003198:Computer Simulation; D019281:Dimerization; D008956:Models, Chemical; D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000737:chemistry / Q000648:ultrastructure; D049329:Nanostructures / Q000737:chemistry* / Q000648:ultrastructure*; D010316:Particle Size; D011487:Protein Conformation; D016944:Sulfolobus / Q000737:chemistry*
D046912:Multiprotein Complexes; D018833:Chaperonins