We present SS-map, a tool to visualize the secondary structure content of ensembles of proteins. When generating ensembles of intrinsically disordered proteins, we lose the understanding a single native structure gives for folded proteins. It then becomes difficult to visualize the composition of the ensembles or to detect transient helices such as MoRFs. Conformational propensities for single residues also hide the nature of cooperative structures. Here we show how SS-map describes folded and unfolded ensembles of some peptides and gives a new view of the ensembles used to describe intrinsically disordered proteins with residual structure in computational and NMR experiments. This tool is implemented in an open-source python code located at code.google.com/p/ss-map.
CITATION STYLE
Iglesias, J., Sanchez-Martínez, M., & Crehuet, R. (2013). SS-map. Intrinsically Disordered Proteins, 1(1), e25323. https://doi.org/10.4161/idp.25323
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