Monitoring protein conformational changes and dynamics using stable-isotope labeling and mass spectrometry
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Biochemistry, Genetics and Molecular Biology
Link
https://www.nature.com/articles/nprot.2014.075.pdf
Reference71 articles.
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2. Kajihara, D. et al. FRET analysis of protein conformational change through position-specific incorporation of fluorescent amino acids. Nat. Methods 3, 923–929 (2006).
3. Taraska, J.W., Puljung, M.C., Olivier, N.B., Flynn, G.E. & Zagotta, W.N. Mapping the structure and conformational movements of proteins with transition metal ion FRET. Nat. Methods 6, 532–537 (2009).
4. Islas, L.D. & Zagotta, W.N. Short-range molecular rearrangements in ion channels detected by tryptophan quenching of bimane fluorescence. J. Gen. Physiol. 128, 337–346 (2006).
5. Ghanouni, P., Steenhuis, J.J., Farrens, D.L. & Kobilka, B.K. Agonist-induced conformational changes in the G-protein–coupling domain of the β2 adrenergic receptor. Proc. Natl. Acad. Sci. USA 98, 5997–6002 (2001).
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