This chapter aims at providing an exhaustive list of methods currently available to detect and characterize intrinsic disorder in proteins. For each method, we briefly describe the principle and discuss the advantages and limitations. Alongside readily available methods, we describe less common and more demanding approaches that enable achieving further insights into the conformational properties of intrinsically disordered proteins (IDPs). The chapter ends with a brief description of methods to model conformational ensembles and to assess protein–protein interaction involving IDPs.
Gondelaud, F., Schramm, A., Brocca, S., Natalello, A., Grandori, R., Santambrogio, C., et al. (2022). Methods for measuring structural disorder in proteins. In M.N. Gupta, V.N. Uversky (a cura di), Structure and Intrinsic Disorder in Enzymology (pp. 149-198). Elsevier [10.1016/B978-0-323-99533-7.00018-2].
Methods for measuring structural disorder in proteins
Brocca S.;Natalello A.;Grandori R.;Santambrogio C.;Longhi S.
2022
Abstract
This chapter aims at providing an exhaustive list of methods currently available to detect and characterize intrinsic disorder in proteins. For each method, we briefly describe the principle and discuss the advantages and limitations. Alongside readily available methods, we describe less common and more demanding approaches that enable achieving further insights into the conformational properties of intrinsically disordered proteins (IDPs). The chapter ends with a brief description of methods to model conformational ensembles and to assess protein–protein interaction involving IDPs.
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