Site-directed spin labeling

Site-directed spin labeling (SDSL) is a technique for investigating the structure and local dynamics of proteins using electron spin resonance. The theory of SDSL is based on the specific reaction of spin labels with amino acids. A spin label's built-in protein structure can be detected by EPR spectroscopy. SDSL is also a useful tool in examinations of the protein folding process.^[1]

^ Oda, Michael N (2003). "The C-terminal domain of apolipoprotein A-I contains a lipid-sensitive conformational trigger". Nature Structural & Molecular Biology. 10 (6): 455–60. doi:10.1038/nsb931. PMID 12754494. S2CID 25438936.

[1] Oda, Michael N (2003). "The C-terminal domain of apolipoprotein A-I contains a lipid-sensitive conformational trigger". Nature Structural & Molecular Biology. 10 (6): 455–60. doi:10.1038/nsb931. PMID 12754494. S2CID 25438936.

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