Physics – Condensed Matter – Soft Condensed Matter
Scientific paper
2008-02-14
Physical Review E 80, 031922 (2009)
Physics
Condensed Matter
Soft Condensed Matter
Minor changes in the presentation
Scientific paper
10.1103/PhysRevE.80.031922
Protein aggregation in the form of amyloid fibrils has important biological and technological implications. Although the self-assembly process is highly efficient, aggregates not in the fibrillar form would also occur and it is important to include these disordered species when discussing the thermodynamic equilibrium behavior of the system. Here, we initiate such a task by considering a mixture of monomeric proteins and the corresponding aggregates in the disordered form (micelles) and in the fibrillar form (amyloid fibrils). Starting with a model on the respective binding free energies for these species, we calculate their concentrations at thermal equilibrium. We then discuss how the incorporation of the disordered structure furthers our understanding on the various amyloid promoting factors observed empirically, and on the kinetics of fibrilization.
No associations
LandOfFree
Self-assembly of protein amyloid: a competition between amorphous and ordered aggregation does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.
If you have personal experience with Self-assembly of protein amyloid: a competition between amorphous and ordered aggregation, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Self-assembly of protein amyloid: a competition between amorphous and ordered aggregation will most certainly appreciate the feedback.
Profile ID: LFWR-SCP-O-682436