書誌事項
- 公開日
- 2013-03
- 資源種別
- journal article
- 権利情報
-
- https://www.elsevier.com/tdm/userlicense/1.0/
- https://www.elsevier.com/legal/tdmrep-license
- DOI
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- 10.1016/j.abb.2012.11.016
- 公開者
- Elsevier BV
この論文をさがす
説明
The unique role of pressure in protein folding studies is emphasized. Variable-pressure NMR experiments carried out under equilibrium conditions give unique opportunities to explore the energy landscape for protein folding. Intermediate conformers that may appear transiently in the kinetic folding experiments may be stably trapped under pressure, allowing examination of their conformations in site-specific detail with modern NMR spectroscopy. The intimate relationship between the kinetic folding experiment and the equilibrium pressure experiment is described with examples from ubiquitin and hen lysozyme.
収録刊行物
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- Archives of Biochemistry and Biophysics
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Archives of Biochemistry and Biophysics 531 (1-2), 110-115, 2013-03
Elsevier BV
