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Testing the paradigm that the denaturing effect of urea on protein stability is offset by methylamines at the physiological concentration ratio of 2:1 (urea:methylamines).

Testing the paradigm that the denaturing effect of urea on protein stability is offset by methylamines at the physiological concentration ratio of 2:1 (urea:methylamines). Research Abstract Details 

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  • Testing the paradigm that the denaturing effect of urea on protein stability is offset by methylamines at the physiological concentration ratio of 2:1 (urea:methylamines). Abstract Text:

    laishram rajendrakumar singhLaishram Rajendrakumar Singh,tanveer ali darTanveer Ali Dar,inamul haqueInamul Haque,farah anjumFarah Anjum,ali akbar moosavi-movahediAli Akbar Moosavi-Movahedi,faizan ahmadFaizan Ahmad,laishram rajendrakumar singhLaishram Rajendrakumar Singh,tanveer ali darTanveer Ali Dar,inamul haqueInamul Haque,farah anjumFarah Anjum,ali akbar moosavi-movahediAli Akbar Moosavi-Movahedi,faizan ahmadFaizan Ahmad,

    The intra- and extracellular urea concentration in many organisms is sufficiently high to destabilize (inhibit) many proteins, yet organisms survive and function. The generally accepted explanation is the counteracting hypothesis, which holds that methylamines stabilize proteins and oppose the deleterious effect of urea. The two osmolytes are typically found at 2:1 concentration ratio (urea:methylamine) under physiological conditions. Does this mean that this ratio holds for all proteins in a cell? The present study tests the counteracting hypothesis by determining the effects of urea and methylamines (trimethylamine N-oxide and sarcosine), singly and in combination at a concentration ratio of 2:1 (urea:methylamine) on the thermal denaturation equilibrium, native state<-->denatured state of three different proteins (alpha-lactalbumin, lysozyme and Ribonuclease-A). We show here that the molar concentration of a methylamine required to offset the denaturing effect of urea at a given concentration is different for different proteins.

    Testing the paradigm that the denaturing effect of urea on protein stability is offset by methylamines at the physiological concentration ratio of 2:1 (urea:methylamines). Publishing Authors By Initials

    lr singhLR Singh,t ali darT Ali Dar,i haqueI Haque,f anjumF Anjum,aa moosavi-movahediAA Moosavi-Movahedi,f ahmadF Ahmad,lr singhLR Singh,t ali darT Ali Dar,i haqueI Haque,f anjumF Anjum,aa moosavi-movahediAA Moosavi-Movahedi,f ahmadF Ahmad,

    For similar abstracts research abstracts see: abstracts research

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    Testing the paradigm that the denaturing effect of urea on protein stability is offset by methylamines at the physiological concentration ratio of 2:1 (urea:methylamines). Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Biochimica et biophysica acta

    VOLUME: 1774

    Page Numbers: 1555-62

    Journal Abbreviation: Biochim. Biophys. Acta

    ISSN: 0006-3002

    DAY: 26

    MONTH: 09

    YEAR: 2007

    Testing the paradigm that the denaturing effect of urea on protein stability is offset by methylamines at the physiological concentration ratio of 2:1 (urea:methylamines). Information

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    LANGUAGE: eng

    NlmUniqueID: 217513

    Testing the paradigm that the denaturing effect of urea on protein stability is offset by methylamines at the physiological concentration ratio of 2:1 (urea:methylamines). Keywords Mesh Terms:

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    Grant and Affiliation Information for Testing the paradigm that the denaturing effect of urea on protein stability is offset by methylamines at the physiological concentration ratio of 2:1 (urea:methylamines).

    AFFILIATION: Department of Biosciences, Jamia Millia Islamia, Jamia Nagar, New Delhi 110 025, India.

    Country: Netherlands

    Netherlands Research PublicationNetherlands Research Publication

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    MEDLINETA: Biochim Biophys Acta

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