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Simultaneous quantification of protein order and disorder using NMR spectroscopy

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Sormanni, Pietro | Piovesan, Damiano | Heller, Gabriella, T | Bonomi, Massimiliano | Kukic, Predrag | Camilloni, Carlo | Fuxreiter, Monika | Dosztanyi, Zsuzsanna | Pappu, Rohit | Madan Babu, M | Longhi, Sonia | Tompa, Peter | Dunker, A, Keith | Uversky, Vladimir, N | Tosatto, Silvio, C E | Vendruscolo, Michele

Edité par CCSD ; Nature Publishing Group -

International audience. Nuclear magnetic resonance spectroscopy is transforming our view of proteins by revealing how their structures and dynamics are closely intertwined to underlie their functions and interactions. Effective descriptions of protein dynamics are uncovering the presence and biological relevance of highly heterogeneous conformational states of proteins, which go beyond the traditional dichotomy between order and disorder by spanning the continuum between them.

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