Conformational Properties of Unfolded HypF-N
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- 作者：Yujie Chen ; Claudia Parrini ; Niccol Taddei ; Lisa J. Lapidus
- 刊名：Journal of Physical Chemistry B
- 出版年：2009
- 出版时间：December 17, 2009
- 年：2009
- 卷：113
- 期：50
- 页码：16209-16213
- 全文大小：256K
- 年卷期：v.113,no.50(December 17, 2009)
- ISSN：1520-5207
文摘
We have measured the intramolecular diffusion rate between distant residues in the aggregation-prone protein HypF-N under various denaturing conditions. Using the method of cysteine quenching of the tryptophan triplet state, we find that intramolecular diffusion remains roughly constant at high concentrations of denaturant (2−6 M GdnHCl) and slows down at low concentrations of denaturant, but the decrease is not uniform throughout the chain. Extrapolation of these measurements to 0 M GdnHCl gives D 10−7 cm2 s−1, about 1 order of magnitude lower than unstructured peptides and at least 2 orders of magnitude higher than well-behaved proteins. This suggests that there is a dynamic range of conformational reorganization within which partially unfolded states are prone to aggregation.