| Форма представления | Статьи в зарубежных журналах и сборниках |
| Год публикации | 2014 |
| Язык | английский |
|
Сироткин Владимир Александрович, автор
|
|
Хадиуллина Айгуль Вакильевна, автор
|
| Библиографическое описание на языке оригинала |
Sirotkin, V.A. A study of the hydration of ribonuclease A using densitometry: Effect of the protein hydrophobicity and polarity. / V.A. Sirotkin, A.V. Khadiullina // Chemical Physics Letters. – 2014. – V.603. – P. 13-17. |
| Аннотация |
The excess volumes of the binary system of ribonuclease A (RNase A) with water were obtained as a function of composition at 25 ?C. The excess quantities for RNase A were compared with the published data for several unrelated proteins (lysozyme, serum albumin, lactoglobulin, and chymotrypsinogen A). The hydrophobicity of these proteins is gradually changed over a wide range. It was found that the more hydrophilic a protein is, the more significant the hydrophilic hydration contribution is. RNase A is the most hydrophilic protein in the present study, and it has the most significant hydrophilic hydration contribution. |
| Ключевые слова |
Ribonuclease A, volume, water, hydration, hydrophobicity, protein, polarity |
| Название журнала |
Chemical Physics Letters
|
| URL |
http://www.sciencedirect.com/science/article/pii/S0009261414002991 |
| Пожалуйста, используйте этот идентификатор, чтобы цитировать или ссылаться на эту карточку |
https://repository.kpfu.ru/?p_id=92570 |
| Файлы ресурса | |
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Полная запись метаданных  |
| Поле DC |
Значение |
Язык |
| dc.contributor.author |
Сироткин Владимир Александрович |
ru_RU |
| dc.contributor.author |
Хадиуллина Айгуль Вакильевна |
ru_RU |
| dc.date.accessioned |
2014-01-01T00:00:00Z |
ru_RU |
| dc.date.available |
2014-01-01T00:00:00Z |
ru_RU |
| dc.date.issued |
2014 |
ru_RU |
| dc.identifier.citation |
Sirotkin, V.A. A study of the hydration of ribonuclease A using densitometry: Effect of the protein hydrophobicity and polarity. / V.A. Sirotkin, A.V. Khadiullina // Chemical Physics Letters. – 2014. – V.603. – P. 13-17. |
ru_RU |
| dc.identifier.uri |
https://repository.kpfu.ru/?p_id=92570 |
ru_RU |
| dc.description.abstract |
Chemical Physics Letters |
ru_RU |
| dc.description.abstract |
The excess volumes of the binary system of ribonuclease A (RNase A) with water were obtained as a function of composition at 25 ?C. The excess quantities for RNase A were compared with the published data for several unrelated proteins (lysozyme, serum albumin, lactoglobulin, and chymotrypsinogen A). The hydrophobicity of these proteins is gradually changed over a wide range. It was found that the more hydrophilic a protein is, the more significant the hydrophilic hydration contribution is. RNase A is the most hydrophilic protein in the present study, and it has the most significant hydrophilic hydration contribution. |
ru_RU |
| dc.language.iso |
ru |
ru_RU |
| dc.subject |
Ribonuclease A |
ru_RU |
| dc.subject |
volume |
ru_RU |
| dc.subject |
water |
ru_RU |
| dc.subject |
hydration |
ru_RU |
| dc.subject |
hydrophobicity |
ru_RU |
| dc.subject |
protein |
ru_RU |
| dc.subject |
polarity |
ru_RU |
| dc.title |
A study of the hydration of ribonuclease A using densitometry: Effect of the protein hydrophobicity and polarity. |
ru_RU |
| dc.type |
Статьи в зарубежных журналах и сборниках |
ru_RU |
|
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