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Kinetic and equilibrium folding intermediatesстатья
- Авторы: Ptitsyn O.B., Bychkova V.E., Uversky V.N.
- Журнал: Philosophical Transactions of the Royal Society B: Biological Sciences
- Том: 348
- Номер: 1323
- Год издания: 1995
- Издательство: Royal Society of London
- Местоположение издательства: United Kingdom
- Первая страница: 35
- Последняя страница: 41
- DOI: 10.1098/rstb.1995.0043
- Аннотация: Our recent experiments on the molten globule state and other protein folding intermediates lead to following conclusions: (i) the molten globule is separated by intramolecular first-order phase transitions from the native and unfolded states and therefore is a specific thermodynamic state of protein molecules; (ii) the novel equilibrium folding intermediate (the 'pre-molten globule' state) exists which can be similar to the 'burst' kinetic intermediate of protein folding; (iii) proteins denature and release their non-polar ligands at moderately low pH and moderately low dielectric constant, i.e. under conditions which may be related to those near membranes.
- Добавил в систему: Уверский Владимир Николаевич