書誌事項
- 公開日
- 2015-01-20
- 権利情報
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- https://www.cambridge.org/core/terms
- DOI
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- 10.1017/s0033583514000122
- 公開者
- Cambridge University Press (CUP)
この論文をさがす
説明
<jats:title>Abstract</jats:title><jats:p>Myriad biological processes proceed through states that defy characterization by conventional atomic-resolution structural biological methods. The invisibility of these ‘dark’ states can arise from their transient nature, low equilibrium population, large molecular weight, and/or heterogeneity. Although they are invisible, these dark states underlie a range of processes, acting as encounter complexes between proteins and as intermediates in protein folding and aggregation. New methods have made these states accessible to high-resolution analysis by nuclear magnetic resonance (NMR) spectroscopy, as long as the dark state is in dynamic equilibrium with an NMR-visible species. These methods – paramagnetic NMR, relaxation dispersion, saturation transfer, lifetime line broadening, and hydrogen exchange – allow the exploration of otherwise invisible states in exchange with a visible species over a range of timescales, each taking advantage of some unique property of the dark state to amplify its effect on a particular NMR observable. In this review, we introduce these methods and explore two specific techniques – paramagnetic relaxation enhancement and dark state exchange saturation transfer – in greater detail.</jats:p>
収録刊行物
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- Quarterly Reviews of Biophysics
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Quarterly Reviews of Biophysics 48 (1), 35-116, 2015-01-20
Cambridge University Press (CUP)