The chemical shift index or CSI is a widely employed technique in protein nuclear magnetic resonance spectroscopy that can be used to display and identify the location (i.e. start and end) as well as the type of protein secondary structure (beta strands, helices and random coil regions) found in proteins using only backbone chemical shift data [1][2] The technique was invented by David S. Wishart in 1992 for analyzing 1Hα chemical shifts and then later extended by him in 1994 to incorporate 13C backbone shifts. The original CSI method makes use of the fact that 1Hα chemical shifts of amino acid residues in helices tends to be shifted upfield (i.e. towards the right side of an NMR spectrum) relative to their random coil values and downfield (i.e. towards the left side of an NMR spectrum) in beta strands. Similar kinds of upfield and downfield trends are also detectable in backbone 13C chemical shifts.
^Wishart DS, Sykes BD, Richards FM (February 1992). "The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy". Biochemistry. 31 (6): 1647–51. CiteSeerX 10.1.1.539.2952. doi:10.1021/bi00121a010. PMID 1737021.
^Wishart, David S.; Sykes, Brian D. (1994). "The 13C Chemical-Shift Index: A simple method for the identification of protein secondary structure using 13C chemical-shift data". Journal of Biomolecular NMR. 4 (2): 171–80. doi:10.1007/BF00175245. PMID 8019132. S2CID 42323147.
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