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Интеллектуальная Система Тематического Исследования НАукометрических данных |
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Triple point mutation Asp10 - His, Asn101 - Asp, Argl48 - Ser in T4 phage lysozyme leads to the molten globuleстатья
- Авторы: Uversky Vladimir N., Leontiev Vladimir V., Gudkov Anatoly T.
- Журнал: Protein engineering
- Том: 5
- Номер: 8
- Год издания: 1992
- Издательство: Oxford University Press
- Местоположение издательства: United Kingdom
- Первая страница: 781
- Последняя страница: 783
- DOI: 10.1093/protein/5.8.781
- Аннотация: The triple amino acid replacement (Asp10-->His, Asn101-->Asp, Arg148-->Ser) in T4 phage lysozyme was carried out by site-directed mutagenesis. At acid pH (2.7) the mutant is in a conformational state with the properties of the molten globule: (i) the mutant protein molecule is essentially compact; (ii) its CD spectrum in the near UV region is drastically reduced in intensity as compared with the wild type protein spectrum; (iii) the CD spectrum in the far UV region indicates the presence of pronounced secondary structure in the mutant; (iv) unlike the wild type protein the mutant protein can bind the hydrophobic fluorescent probe, ANS.
- Добавил в систему: Уверский Владимир Николаевич