Temperature-dependent dielectric relaxation and hydrophobicity of aqueous alanine using time domain reflectometry
| Autor: | Suad Alwaleedy, Saeed Mohemmed, Ravi Karale, Komal Kabara, Ashok Kumbharkhane, Bunty Roy, Arvind Sarode |
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| Rok vydání: | 2022 |
| Předmět: | |
| Zdroj: | Journal of Biomolecular Structure and Dynamics. :1-12 |
| ISSN: | 1538-0254 0739-1102 |
| DOI: | 10.1080/07391102.2022.2157877 |
| Popis: | Physical, chemical and microbiological stability of the materials is affected by the rotational and translational mobility of free and hydrated water. The role of water in areas such as protein hydration and enzyme activity, food technology, lyophilization and polymers hydration is, therefore, important and can be well understood in terms of dielectric relaxation spectroscopy. Concentration and temperature-dependent hydrophobicity of amino acid is reflected in their tendencies to appear in appropriate positions in proteins. Therefore, to gain more insights on the temperature and concentration dependence of hydrophobicity and structural properties of amino acid, dielectric relaxation of aqueous alanine have been studied in the temperature region 303.15 K to 278.15 K. Time domain spectroscopy have been used in the frequency range of 10 MHz to 30 GHz and in the concentration range 0.18708 ≤ |
| Databáze: | OpenAIRE |
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