ncSPC is a program that calculates the structural propensities for folded and (intrinsically) disordered proteins from NMR chemical shift data. The program then calculates the extent of alpha-helical and beta-strand formed at each residue in the sequence. The program uses random coil reference data from ncIDP (Tamiola K, Acar B, Mulder FA. J Am Chem Soc. 2010 Dec 29;132(51):18000-3) and an algorithm for converting the measured data into secondary structure propensities (Marsh JA, Singh VK, Jia Z, Forman-Kay JD. Protein Sci. 2006 Dec;15(12):2795-804). Taking neighbor corrections into account significantly increases the accuracy of the method, hence the abbreviation ‘nc’ at the beginning of its name.


Using NMR chemical shifts to calculate the propensity for structural order and disorder in proteins. Tamiola K, Mulder FAA. Biochem Soc Trans. 2012 Oct;40(5):1014-20.
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