Abstract
5. ConclusionIn summary, SDSL is rapidly becoming a mature technique with which to approach questions related to structure-function relationships in proteins. This ESR method is uniquely suited to membrane proteins, and it can provide information on systems that are not amenable to modern NMR and crystallographic methods. SDSL methods are adept at defining local secondary structure (e.g., α-helix and β-strand) through nitroxide-scanning experiments and the sensitivity of the ESR spin label spectrum to molecular motion can give insights into both local and global conformational changes that accompany such events as ligand binding and denaturation. Continued improvements in methods for making distance measurements for both nitroxide: nitroxide and metal: nitroxide pairs will enhance the future application of the site-directed spin-labeling approach even further.
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