Quantification of free cysteines in membrane and soluble proteins using a fluorescent dye and thermal unfolding-Reference-Cited by-同舟云学术

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Quantification of free cysteines in membrane and soluble proteins using a fluorescent dye and thermal unfolding

Published:2013-10-03 Issue:11 Volume:8 Page:2090-2097
ISSN:1754-2189
Container-title:Nature Protocols
language:en
Short-container-title:Nat Protoc

Author:

Branigan Emma,Pliotas Christos,Hagelueken Gregor,Naismith James H

Publisher

Springer Science and Business Media LLC

Subject

General Biochemistry, Genetics and Molecular Biology

Link

https://www.nature.com/articles/nprot.2013.128.pdf

Reference28 articles.

1. Hoff, A.J. Advanced EPR. Applications in Biology and Biochemistry (Elsevier, 1989).

2. Powl, A.M., Wright, J.N., East, J.M. & Lee, A.G. Identification of the hydrophobic thickness of a membrane protein using fluorescence spectroscopy: studies with the mechanosensitive channel MscL. Biochemistry 44, 5713–5721 (2005).

3. Hubbell, W.L., Cafiso, D.S. & Altenbach, C. Identifying conformational changes with site-directed spin labeling. Nat. Struct. Biol. 7, 735–739 (2000).

4. Chalker, J.M., Bernardes, G.J.L., Lin, Y.A. & Davis, B.G. Chemical modification of proteins at cysteine: opportunities in chemistry and biology. Chem. Asian J. 4, 630–640 (2009).

5. Ellman, G.L. Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82, 70–77 (1959).

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