Simultaneous Quantification of Protein Order and Disorder
Document Type
Article
Publication Date
2017
Keywords
Protein folding, Structural biology
Digital Object Identifier (DOI)
https://doi.org/10.1038/nchembio.2331
Abstract
Nuclear magnetic resonance spectroscopy is transforming our views of proteins by revealing how their structures and dynamics are closely intertwined to underlie their functions and interactions. Compelling representations of proteins as statistical ensembles are uncovering the presence and biological relevance of conformationally heterogeneous states, thus gradually making it possible to go beyond the dichotomy between order and disorder through more quantitative descriptions that span the continuum between them.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Nature Chemical Biology, v. 13, p. 339-342
Scholar Commons Citation
Sormanni, Pietro; Piovesan, Damiano; Heller, Gabriella T.; Bonomi, Massimiliano; Kukic, Predrag; Camilloni, Carlo; Fuxreiter, Monika; Dosztanyi, Zsuzsanna; Pappu, Rohit V.; Babu, M Madan; Longhi, Sonia; Tompa, Peter; Dunker, A Keith; Uversky, Vladimir N.; Tosatto, Silvio C.; and Vendruscolo, Michele, "Simultaneous Quantification of Protein Order and Disorder" (2017). Molecular Medicine Faculty Publications. 318.
https://digitalcommons.usf.edu/mme_facpub/318
