Characterization of Dynamic IDP Complexes by NMR Spectroscopy

Publikation: Bidrag til bog/antologi/rapportBidrag til bog/antologiForskningfagfællebedømt

NMR spectroscopy has proven to be a key method for studying intrinsically disordered proteins (IDPs). Nonetheless, traditional NMR methods developed for solving structures of ordered protein complexes are insufficient for the full characterization of dynamic IDP complexes, where the energy landscape is broader and more rugged. Furthermore, due to their high sensitivity to environmental changes, NMR studies of IDP complexes must be conducted with extra care and the observed NMR parameters thoroughly evaluated to enable disentanglement of binding events from ensemble distribution changes. In this chapter, written for the non-NMR expert, we start out by outlining sample preparation for IDP complexes, guide through the recording and evaluation of diagnostic 1H,15N-HSQC spectra, and delineate more sophisticated NMR strategies to follow for the particular type of complex. The most relevant experiments are then described in terms of aims, needs, pitfalls, analysis, and expected outcomes, with references to recent examples.

OriginalsprogEngelsk
TitelIntrinsically Disordered Proteins
RedaktørerElizabeth Rhoades
Antal sider34
ForlagAcademic Press
Publikationsdato2018
Sider193-226
Kapitel8
ISBN (Trykt)978-0-12-815649-0
DOI
StatusUdgivet - 2018
NavnMethods in Enzymology
Vol/bind611
ISSN0076-6879

ID: 209705679