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CIDER and localCIDER make use of parameters defined in a number of papers. We strongly recommend reading those papers for further details on the parameters being calculated here, and their correct usage and interpretation.

[1] TOP-IDP-scale: a new amino acid scale measuring propensity for intrinsic disorder
Campen, A., Williams, R.M., Brown, C.J., Meng, J., Uversky, V.N., Dunker, A.K. (2008)
Protein Pept Lett. 15(9) pp 956 - 963
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[2] Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues
Das, R.K. & Pappu, R.V. (2013)
PNAS 110, 33, pp 13392 - 13397
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[3] A simple method for displaying the hydropathic character of a protein.
Kyte, J. & Doolittle, R. (1982)
J. Mol. Biol. 157, pp 105 - 132
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[4] Natively unfolded proteins: A point where biology waits for physics
Uversky, V. (2002)
Protein Sci. Apr 11(4), pp 739 - 756
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[5] Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation
Martin, E.W.*, Holehouse, A.S.*, Grace, C.R., Hughes, A., Pappu, R.V., and Mittag, T. (2016)
J. Am. Chem. Soc. 138, pp 15323 - 15335
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