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Thermodynamic implications of high Q(10) of thermo-TRP channels in living cells
The activity of thermo-transient receptor potential (TRP) channels is highly dependent on temperature, and thus thermo-TRP reactions have a high temperature coefficient Q(10). In thermodynamics, a high value of Q(10) indicates the existence of a large activation energy (i.e., a large enthalpy) over...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Biophysical Society of Japan (BSJ)
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4736789/ https://www.ncbi.nlm.nih.gov/pubmed/27493512 http://dx.doi.org/10.2142/biophysics.11.33 |
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author | Ito, Etsuro Ikemoto, Yusuke Yoshioka, Tohru |
author_facet | Ito, Etsuro Ikemoto, Yusuke Yoshioka, Tohru |
author_sort | Ito, Etsuro |
collection | PubMed |
description | The activity of thermo-transient receptor potential (TRP) channels is highly dependent on temperature, and thus thermo-TRP reactions have a high temperature coefficient Q(10). In thermodynamics, a high value of Q(10) indicates the existence of a large activation energy (i.e., a large enthalpy) over a short period during the transition process between the closed and open states of the channels. The Gibbs free energy equation shows that a large entropy is required to compensate for this large enthalpy and permit activation of the channels, suggesting a large conformational change of the channels. These large values of enthalpy and entropy seem to be a match for the values of the unfolding process of globular proteins. We outline these thermodynamic issues in thermo-TRPs. |
format | Online Article Text |
id | pubmed-4736789 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The Biophysical Society of Japan (BSJ) |
record_format | MEDLINE/PubMed |
spelling | pubmed-47367892016-08-04 Thermodynamic implications of high Q(10) of thermo-TRP channels in living cells Ito, Etsuro Ikemoto, Yusuke Yoshioka, Tohru Biophysics (Nagoya-shi) Note The activity of thermo-transient receptor potential (TRP) channels is highly dependent on temperature, and thus thermo-TRP reactions have a high temperature coefficient Q(10). In thermodynamics, a high value of Q(10) indicates the existence of a large activation energy (i.e., a large enthalpy) over a short period during the transition process between the closed and open states of the channels. The Gibbs free energy equation shows that a large entropy is required to compensate for this large enthalpy and permit activation of the channels, suggesting a large conformational change of the channels. These large values of enthalpy and entropy seem to be a match for the values of the unfolding process of globular proteins. We outline these thermodynamic issues in thermo-TRPs. The Biophysical Society of Japan (BSJ) 2015-02-13 /pmc/articles/PMC4736789/ /pubmed/27493512 http://dx.doi.org/10.2142/biophysics.11.33 Text en 2015 © The Biophysical Society of Japan This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Note Ito, Etsuro Ikemoto, Yusuke Yoshioka, Tohru Thermodynamic implications of high Q(10) of thermo-TRP channels in living cells |
title | Thermodynamic implications of high Q(10) of thermo-TRP channels in living cells |
title_full | Thermodynamic implications of high Q(10) of thermo-TRP channels in living cells |
title_fullStr | Thermodynamic implications of high Q(10) of thermo-TRP channels in living cells |
title_full_unstemmed | Thermodynamic implications of high Q(10) of thermo-TRP channels in living cells |
title_short | Thermodynamic implications of high Q(10) of thermo-TRP channels in living cells |
title_sort | thermodynamic implications of high q(10) of thermo-trp channels in living cells |
topic | Note |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4736789/ https://www.ncbi.nlm.nih.gov/pubmed/27493512 http://dx.doi.org/10.2142/biophysics.11.33 |
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