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Thermodynamic properties of amyloid fibrils in equilibrium
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 prote...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5589490/ https://www.ncbi.nlm.nih.gov/pubmed/28318905 http://dx.doi.org/10.1016/j.bpc.2017.03.001 |
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author | Urbic, Tomaz Najem, Sara Dias, Cristiano L. |
author_facet | Urbic, Tomaz Najem, Sara Dias, Cristiano L. |
author_sort | Urbic, Tomaz |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-5589490 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
record_format | MEDLINE/PubMed |
spelling | pubmed-55894902018-12-01 Thermodynamic properties of amyloid fibrils in equilibrium Urbic, Tomaz Najem, Sara Dias, Cristiano L. Biophys Chem Article 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. 2017-03-07 2017-12 /pmc/articles/PMC5589490/ /pubmed/28318905 http://dx.doi.org/10.1016/j.bpc.2017.03.001 Text en http://creativecommons.org/licenses/by-nc-nd/4.0/ This manuscript version is made available under the CC BY-NC-ND 4.0 license. |
spellingShingle | Article Urbic, Tomaz Najem, Sara Dias, Cristiano L. Thermodynamic properties of amyloid fibrils in equilibrium |
title | Thermodynamic properties of amyloid fibrils in equilibrium |
title_full | Thermodynamic properties of amyloid fibrils in equilibrium |
title_fullStr | Thermodynamic properties of amyloid fibrils in equilibrium |
title_full_unstemmed | Thermodynamic properties of amyloid fibrils in equilibrium |
title_short | Thermodynamic properties of amyloid fibrils in equilibrium |
title_sort | thermodynamic properties of amyloid fibrils in equilibrium |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5589490/ https://www.ncbi.nlm.nih.gov/pubmed/28318905 http://dx.doi.org/10.1016/j.bpc.2017.03.001 |
work_keys_str_mv | AT urbictomaz thermodynamicpropertiesofamyloidfibrilsinequilibrium AT najemsara thermodynamicpropertiesofamyloidfibrilsinequilibrium AT diascristianol thermodynamicpropertiesofamyloidfibrilsinequilibrium |