Thermodynamic properties of amyloid fibrils in equilibrium

被引：11
|
作者：
Urbic, Tomaz [1 ]
Najem, Sara [2 ]
Dias, Cristiano L. [3 ]
机构：
[1] Univ Ljubljana, Fac Chem & Chem Technol, Vecna Pot 113, Ljubljana 1000, Slovenia
[2] Natl Council Sci Res, Natl Ctr Remote Sensing, CNRS, Beirut 11072260, Lebanon
[3] New Jersey Inst Technol, Phys Dept, Newark, NJ 07042 USA
来源：
BIOPHYSICAL CHEMISTRY | 2017年 / 231卷
关键词：
COMPUTER-SIMULATIONS; AGGREGATION KINETICS; 2-DIMENSIONAL MODEL; COLD DENATURATION; PROTEIN; CALORIMETRY; ENERGETICS; STABILITY; WATER; NUCLEATION;
D O I：
10.1016/j.bpc.2017.03.001
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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. (C) 2017 Elsevier B.V. All rights reserved.
引用
收藏
页码：155 / 160
页数：6
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