TY - JOUR
T1 - Thermodynamic properties of amyloid fibrils in equilibrium
AU - Urbic, Tomaz
AU - Najem, Sara
AU - Dias, Cristiano L.
N1 - Funding Information:
T. U. are grateful for the support of the NIH ( GM063592 ) and Slovenian Research Agency ( P1 0103-0201 , N1-0042 ) and the National Research, Development and Innovation Office of Hungary ( SNN 116198 ). Appendix A
Publisher Copyright:
© 2017 Elsevier B.V.
PY - 2017/12
Y1 - 2017/12
N2 - 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.
AB - 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.
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U2 - 10.1016/j.bpc.2017.03.001
DO - 10.1016/j.bpc.2017.03.001
M3 - Article
C2 - 28318905
AN - SCOPUS:85019690539
SN - 0301-4622
VL - 231
SP - 155
EP - 160
JO - Biophysical Chemistry
JF - Biophysical Chemistry
ER -