Salt potentiates methylamine counteraction system to offset the deleterious effects of urea on protein stability and function.
Cellular methylamines are osmolytes (low molecular weight organic compounds) believed to offset the urea's harmful effects on the stability and function of proteins in mammalian kidney and marine invertebrates. Although urea and methylamines are found at 2:1 molar ratio in tissues, their opposi...
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doaj-5f3d6b72e9a84e31b81f1a6c5f384d692020-11-25T00:51:28ZengPublic Library of Science (PLoS)PLoS ONE1932-62032015-01-01103e011959710.1371/journal.pone.0119597Salt potentiates methylamine counteraction system to offset the deleterious effects of urea on protein stability and function.Safikur RahmanMd Tabish RehmanLaishram R SinghMarina WarepamFaizan AhmadTanveer Ali DarCellular methylamines are osmolytes (low molecular weight organic compounds) believed to offset the urea's harmful effects on the stability and function of proteins in mammalian kidney and marine invertebrates. Although urea and methylamines are found at 2:1 molar ratio in tissues, their opposing effects on protein structure and function have been questioned on several grounds including failure to counteraction or partial counteraction. Here we investigated the possible involvement of cellular salt, NaCl, in urea-methylamine counteraction on protein stability and function. We found that NaCl mediates methylamine counteracting system from no or partial counteraction to complete counteraction of urea's effect on protein stability and function. These conclusions were drawn from the systematic thermodynamic stability and functional activity measurements of lysozyme and RNase-A. Our results revealed that salts might be involved in protein interaction with charged osmolytes and hence in the urea-methylamine counteraction.http://europepmc.org/articles/PMC4368626?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Safikur Rahman Md Tabish Rehman Laishram R Singh Marina Warepam Faizan Ahmad Tanveer Ali Dar |
spellingShingle |
Safikur Rahman Md Tabish Rehman Laishram R Singh Marina Warepam Faizan Ahmad Tanveer Ali Dar Salt potentiates methylamine counteraction system to offset the deleterious effects of urea on protein stability and function. PLoS ONE |
author_facet |
Safikur Rahman Md Tabish Rehman Laishram R Singh Marina Warepam Faizan Ahmad Tanveer Ali Dar |
author_sort |
Safikur Rahman |
title |
Salt potentiates methylamine counteraction system to offset the deleterious effects of urea on protein stability and function. |
title_short |
Salt potentiates methylamine counteraction system to offset the deleterious effects of urea on protein stability and function. |
title_full |
Salt potentiates methylamine counteraction system to offset the deleterious effects of urea on protein stability and function. |
title_fullStr |
Salt potentiates methylamine counteraction system to offset the deleterious effects of urea on protein stability and function. |
title_full_unstemmed |
Salt potentiates methylamine counteraction system to offset the deleterious effects of urea on protein stability and function. |
title_sort |
salt potentiates methylamine counteraction system to offset the deleterious effects of urea on protein stability and function. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2015-01-01 |
description |
Cellular methylamines are osmolytes (low molecular weight organic compounds) believed to offset the urea's harmful effects on the stability and function of proteins in mammalian kidney and marine invertebrates. Although urea and methylamines are found at 2:1 molar ratio in tissues, their opposing effects on protein structure and function have been questioned on several grounds including failure to counteraction or partial counteraction. Here we investigated the possible involvement of cellular salt, NaCl, in urea-methylamine counteraction on protein stability and function. We found that NaCl mediates methylamine counteracting system from no or partial counteraction to complete counteraction of urea's effect on protein stability and function. These conclusions were drawn from the systematic thermodynamic stability and functional activity measurements of lysozyme and RNase-A. Our results revealed that salts might be involved in protein interaction with charged osmolytes and hence in the urea-methylamine counteraction. |
url |
http://europepmc.org/articles/PMC4368626?pdf=render |
work_keys_str_mv |
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