Characterization of Dynamic IDP Complexes by NMR Spectroscopy
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Characterization of Dynamic IDP Complexes by NMR Spectroscopy. / Prestel, Andreas; Bugge, Katrine; Staby, Lasse; Hendus-Altenburger, Ruth; Kragelund, Birthe B.
Intrinsically Disordered Proteins. red. / Elizabeth Rhoades. Academic Press, 2018. s. 193-226 (Methods in Enzymology, Bind 611).Publikation: Bidrag til bog/antologi/rapport › Bidrag til bog/antologi › Forskning › fagfællebedømt
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TY - CHAP
T1 - Characterization of Dynamic IDP Complexes by NMR Spectroscopy
AU - Prestel, Andreas
AU - Bugge, Katrine
AU - Staby, Lasse
AU - Hendus-Altenburger, Ruth
AU - Kragelund, Birthe B.
PY - 2018
Y1 - 2018
N2 - 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.
AB - 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.
KW - Affinity
KW - Dynamics
KW - Fuzzy
KW - Integrative structural biology
KW - Interaction
KW - Intrinsically disordered proteins
KW - Ligand binding
KW - Practical sample preparation
KW - Protein
U2 - 10.1016/bs.mie.2018.08.026
DO - 10.1016/bs.mie.2018.08.026
M3 - Book chapter
C2 - 30471688
AN - SCOPUS:85055664617
SN - 978-0-12-815649-0
T3 - Methods in Enzymology
SP - 193
EP - 226
BT - Intrinsically Disordered Proteins
A2 - Rhoades, Elizabeth
PB - Academic Press
ER -
ID: 209705679