Thermodynamic properties of amyloid fibrils in equilibrium
Document Type
Article
Publication Date
12-1-2017
Abstract
In this manuscript we use a two-dimensional coarse-grained model to study how amyloid fibrils grow towards an equilibrium state where they coexist with proteins dissolved in a solution. Free-energies to dissociate proteins from fibrils are estimated from the residual concentration of dissolved proteins. Consistent with experiments, the concentration of proteins in solution affects the growth rate of fibrils but not their equilibrium state. Also, studies of the temperature dependence of the equilibrium state can be used to estimate thermodynamic quantities, e.g., heat capacity and entropy.
Identifier
85019690539 (Scopus)
Publication Title
Biophysical Chemistry
External Full Text Location
https://doi.org/10.1016/j.bpc.2017.03.001
e-ISSN
18734200
ISSN
03014622
PubMed ID
28318905
First Page
155
Last Page
160
Volume
231
Grant
SNN 116198
Fund Ref
National Institutes of Health
Recommended Citation
Urbic, Tomaz; Najem, Sara; and Dias, Cristiano L., "Thermodynamic properties of amyloid fibrils in equilibrium" (2017). Faculty Publications. 9147.
https://digitalcommons.njit.edu/fac_pubs/9147
