Volumetric and viscometric properties of amino acids in aqueous solutions of various drugs at different temperatures: A review.

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Title: Volumetric and viscometric properties of amino acids in aqueous solutions of various drugs at different temperatures: A review.
Authors: Rani, Ruby1 (AUTHOR) rubysalgotra13@gmail.com, Rajput, Shikha1 (AUTHOR), Sharma, Keshav1 (AUTHOR), Baboria, Vikrant1 (AUTHOR)
Source: Molecular Physics. Feb2022, Vol. 120 Issue 4, p1-20. 20p.
Subjects: Molecular volume, Amino acids, Acid solutions, Aqueous solutions, Protein drugs, Pharmacodynamics
Abstract: This review systematically surveys the limiting apparent molar volume, limiting apparent molar volume of transfer, Hepler's constant, hydration number, viscosity B-coefficients, and temperature derivative of B-coefficients, dB/dT of amino acids in aqueous solution of various drugs at different temperatures as these data are quite important for interpreting the hydration and other properties of proteins. The effect of drug on the volumetric and viscometric properties of amino acids has been discussed in terms of various physicochemical interactions, e.g. ion-ion, ion-hydrophilic, hydrophilic–hydrophilic, hydrophilic–hydrophobic and hydrophobic–hydrophobic interactions. These are also discussed in terms of structure-making/structure-breaking tendency of the amino acids in presence of various drugs. The comparison of these effects on the amino acid hydration enables us to have a better understanding of the influence of drugs on the protein stabilization. [ABSTRACT FROM AUTHOR]
Copyright of Molecular Physics is the property of Taylor & Francis Ltd and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Volumetric and viscometric properties of amino acids in aqueous solutions of various drugs at different temperatures: A review.
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  Data: <searchLink fieldCode="AR" term="%22Rani%2C+Ruby%22">Rani, Ruby</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> rubysalgotra13@gmail.com</i><br /><searchLink fieldCode="AR" term="%22Rajput%2C+Shikha%22">Rajput, Shikha</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Sharma%2C+Keshav%22">Sharma, Keshav</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Baboria%2C+Vikrant%22">Baboria, Vikrant</searchLink><relatesTo>1</relatesTo> (AUTHOR)
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  Data: <searchLink fieldCode="JN" term="%22Molecular+Physics%22">Molecular Physics</searchLink>. Feb2022, Vol. 120 Issue 4, p1-20. 20p.
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  Data: <searchLink fieldCode="DE" term="%22Molecular+volume%22">Molecular volume</searchLink><br /><searchLink fieldCode="DE" term="%22Amino+acids%22">Amino acids</searchLink><br /><searchLink fieldCode="DE" term="%22Acid+solutions%22">Acid solutions</searchLink><br /><searchLink fieldCode="DE" term="%22Aqueous+solutions%22">Aqueous solutions</searchLink><br /><searchLink fieldCode="DE" term="%22Protein+drugs%22">Protein drugs</searchLink><br /><searchLink fieldCode="DE" term="%22Pharmacodynamics%22">Pharmacodynamics</searchLink>
– Name: Abstract
  Label: Abstract
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  Data: This review systematically surveys the limiting apparent molar volume, limiting apparent molar volume of transfer, Hepler's constant, hydration number, viscosity B-coefficients, and temperature derivative of B-coefficients, dB/dT of amino acids in aqueous solution of various drugs at different temperatures as these data are quite important for interpreting the hydration and other properties of proteins. The effect of drug on the volumetric and viscometric properties of amino acids has been discussed in terms of various physicochemical interactions, e.g. ion-ion, ion-hydrophilic, hydrophilic–hydrophilic, hydrophilic–hydrophobic and hydrophobic–hydrophobic interactions. These are also discussed in terms of structure-making/structure-breaking tendency of the amino acids in presence of various drugs. The comparison of these effects on the amino acid hydration enables us to have a better understanding of the influence of drugs on the protein stabilization. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Molecular Physics is the property of Taylor & Francis Ltd and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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RecordInfo BibRecord:
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    Identifiers:
      – Type: doi
        Value: 10.1080/00268976.2021.1992029
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      – Code: eng
        Text: English
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      Pagination:
        PageCount: 20
        StartPage: 1
    Subjects:
      – SubjectFull: Molecular volume
        Type: general
      – SubjectFull: Amino acids
        Type: general
      – SubjectFull: Acid solutions
        Type: general
      – SubjectFull: Aqueous solutions
        Type: general
      – SubjectFull: Protein drugs
        Type: general
      – SubjectFull: Pharmacodynamics
        Type: general
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      – TitleFull: Volumetric and viscometric properties of amino acids in aqueous solutions of various drugs at different temperatures: A review.
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            NameFull: Rani, Ruby
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            NameFull: Rajput, Shikha
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            NameFull: Sharma, Keshav
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            NameFull: Baboria, Vikrant
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            – D: 15
              M: 02
              Text: Feb2022
              Type: published
              Y: 2022
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