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Thermodynamic properties of amyloid fibrils in equilibrium
- Source :
- Biophysical chemistry
- Publication Year :
- 2017
- Publisher :
- Elsevier BV, 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.<br />Graphical abstract
- Subjects :
- 0301 basic medicine
Thermodynamic equilibrium
Physics::Medical Physics
Biophysics
Thermodynamics
Fibril
01 natural sciences
Biochemistry
Heat capacity
Article
03 medical and health sciences
0103 physical sciences
Growth rate
010306 general physics
Quantitative Biology::Biomolecules
Amyloid beta-Peptides
Chemistry
Hydrogen bond
Organic Chemistry
Temperature
Hydrogen Bonding
Amyloid fibril
030104 developmental biology
Physical chemistry
Monte Carlo Method
Subjects
Details
- ISSN :
- 03014622
- Volume :
- 231
- Database :
- OpenAIRE
- Journal :
- Biophysical Chemistry
- Accession number :
- edsair.doi.dedup.....504aecc1cab285819a0b10da088d15f2
- Full Text :
- https://doi.org/10.1016/j.bpc.2017.03.001