Fluorescence-based characterization of non-fluorescent transient states of tryptophan – prospects for protein conformation and interaction studies
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Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/srep35052.pdf
Reference60 articles.
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4. Buscaglia, M., Kubelka, J., Eaton, W. A. & Hofrichter, J. Determination of ultrafast protein folding rates from loop formation dynamics. J. Mol. Biol. 347, 657–664 (2005).
5. Subramaniam, V., Gafni, A. & Steel, D. G. Time-resolved tryptophan phosphorescence spectroscopy: a sensitive probe of protein folding and structure. IEEE J. Selected Topics in Quant. Electron. 2, 1107–1114 (1996).
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