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Association-induced folding of globular proteinsстатья
- Авторы: Uversky Vladimir N., Segel Daniel J., Doniach Sebastian, Fink Anthony L.
- Журнал: Proceedings of the National Academy of Sciences of the United States of America
- Том: 95
- Номер: 10
- Год издания: 1998
- Издательство: National Academy of Sciences
- Местоположение издательства: United States
- Первая страница: 5480
- Последняя страница: 5483
- DOI: 10.1073/pnas.95.10.5480
- Аннотация: It has generally been assumed that the aggregation of partially folded intermediates during protein refolding results in the termination of further protein folding. We show here, however, that under some conditions the association of partially folded intermediates can induce additional structure leading to soluble aggregates with many native-like properties. The amount of secondary structure in a monomeric, partially folded intermediate of staphylococcal nuclease was found to double on formation of soluble aggregates at high protein or salt concentrations. In addition, more globularity, as determined from Kratky plots of small-angle x-ray scattering data, was also noted in the associated states.
- Добавил в систему: Уверский Владимир Николаевич