Salt-specific effects in lysozyme solutions
The effects of additions of low-molecular-mass salts on the properties of aqueous lysozyme solutions are examined by using the cloud-point temperature, Tcloud, measurements. Mixtures of protein, buffer, and simple salt in water are studied at pH=6.8 (phosphate buffer) and pH=4.6 (acetate buffer). We...
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Дата: | 2016 |
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Інститут фізики конденсованих систем НАН України
2016
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Назва видання: | Condensed Matter Physics |
Онлайн доступ: | http://dspace.nbuv.gov.ua/handle/123456789/155805 |
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Назва журналу: | Digital Library of Periodicals of National Academy of Sciences of Ukraine |
Цитувати: | Salt-specific effects in lysozyme solutions / T. Janc, M. Kastelic, M. Bončina, V. Vlachy // Condensed Matter Physics. — 2016. — Т. 19, № 2. — С. 23601: 1–12. — Бібліогр.: 64 назв. — англ. |
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irk-123456789-1558052019-06-18T01:29:44Z Salt-specific effects in lysozyme solutions Janc, T. Kastelic, M. Bončina, M. Vlachy, V. The effects of additions of low-molecular-mass salts on the properties of aqueous lysozyme solutions are examined by using the cloud-point temperature, Tcloud, measurements. Mixtures of protein, buffer, and simple salt in water are studied at pH=6.8 (phosphate buffer) and pH=4.6 (acetate buffer). We show that an addition of buffer in the amount above Ibuffer = 0.6 mol dm⁻³ does not affect the Tcloud values. However, by replacing a certain amount of the buffer electrolyte by another salt, keeping the total ionic strength constant, we can significantly change the cloud-point temperature. All the salts de-stabilize the solution and the magnitude of the effect depends on the nature of the salt. Experimental results are analyzed within the framework of the one-component model, which treats the protein-protein interaction as highly directional and of short-range. We use this approach to predict the second virial coefficients, and liquid-liquid phase diagrams under conditions, where Tcloud is determined experimentally. Ефекти додавання солей з малою молекулярною масою на властивостi водних розчинiв лiзозиму встановлюються з вимiрювань температури точки хмари, Tcloud. Дослiджуються сумiшi протеїну, буферного електролiту i простої солi у водi при pH = 6.8 (фосфатний буфер) i pH = 4.6 (ацетатний буфер). Ми показуємо, що додавання буферного електролiту вище Tbuffer = 0.6 моль дм⁻³ не впливає на значення Tcloud. Однак, при замiнi певної кiлькостi буферного електролiту iншою сiллю, тримаючи постiйною повну iонну мiцнiсть, ми можемо суттєво змiнити температуру точки хмари. Усi солi дестабiлiзують розчин, i величина ефекту залежить вiд природи солi. Експериментальнi результати аналiзуються в рамках однокомпонентної моделi, яка розглядає взаємодiю протеїн-протеїн як сильно направлену та короткодiючу. Ми використовуємо цей пiдхiд для передбачення других вiрiальних коефiцiєнтiв та фазових дiаграм рiдина-рiдина при умовах, коли Tcloud визначається експериментально. 2016 Article Salt-specific effects in lysozyme solutions / T. Janc, M. Kastelic, M. Bončina, V. Vlachy // Condensed Matter Physics. — 2016. — Т. 19, № 2. — С. 23601: 1–12. — Бібліогр.: 64 назв. — англ. 1607-324X DOI:10.5488/CMP.19.23601 arXiv:1603.07114 PACS: 64.60.My, 64.70.Ja, 87.15.km, 87.15.nr, 87.80.Dj http://dspace.nbuv.gov.ua/handle/123456789/155805 en Condensed Matter Physics Інститут фізики конденсованих систем НАН України |
institution |
Digital Library of Periodicals of National Academy of Sciences of Ukraine |
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DSpace DC |
language |
English |
description |
The effects of additions of low-molecular-mass salts on the properties of aqueous lysozyme solutions are examined by using the cloud-point temperature, Tcloud, measurements. Mixtures of protein, buffer, and simple salt in water are studied at pH=6.8 (phosphate buffer) and pH=4.6 (acetate buffer). We show that an addition of buffer in the amount above Ibuffer = 0.6 mol dm⁻³ does not affect the Tcloud values. However, by replacing a certain amount of the buffer electrolyte by another salt, keeping the total ionic strength constant, we can significantly change the cloud-point temperature. All the salts de-stabilize the solution and the magnitude of the effect depends on the nature of the salt. Experimental results are analyzed within the framework of the one-component model, which treats the protein-protein interaction as highly directional and of short-range. We use this approach to predict the second virial coefficients, and liquid-liquid phase diagrams under conditions, where Tcloud is determined experimentally. |
format |
Article |
author |
Janc, T. Kastelic, M. Bončina, M. Vlachy, V. |
spellingShingle |
Janc, T. Kastelic, M. Bončina, M. Vlachy, V. Salt-specific effects in lysozyme solutions Condensed Matter Physics |
author_facet |
Janc, T. Kastelic, M. Bončina, M. Vlachy, V. |
author_sort |
Janc, T. |
title |
Salt-specific effects in lysozyme solutions |
title_short |
Salt-specific effects in lysozyme solutions |
title_full |
Salt-specific effects in lysozyme solutions |
title_fullStr |
Salt-specific effects in lysozyme solutions |
title_full_unstemmed |
Salt-specific effects in lysozyme solutions |
title_sort |
salt-specific effects in lysozyme solutions |
publisher |
Інститут фізики конденсованих систем НАН України |
publishDate |
2016 |
url |
http://dspace.nbuv.gov.ua/handle/123456789/155805 |
citation_txt |
Salt-specific effects in lysozyme solutions / T. Janc, M. Kastelic, M. Bončina, V. Vlachy // Condensed Matter Physics. — 2016. — Т. 19, № 2. — С. 23601: 1–12. — Бібліогр.: 64 назв. — англ. |
series |
Condensed Matter Physics |
work_keys_str_mv |
AT janct saltspecificeffectsinlysozymesolutions AT kastelicm saltspecificeffectsinlysozymesolutions AT boncinam saltspecificeffectsinlysozymesolutions AT vlachyv saltspecificeffectsinlysozymesolutions |
first_indexed |
2023-05-20T17:48:06Z |
last_indexed |
2023-05-20T17:48:06Z |
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1796154124183535616 |