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

Harvard

Prestel, A, Bugge, K, Staby, L, Hendus-Altenburger, R & Kragelund, BB 2018, Characterization of Dynamic IDP Complexes by NMR Spectroscopy. i E Rhoades (red.), Intrinsically Disordered Proteins. Academic Press, Methods in Enzymology, bind 611, s. 193-226. https://doi.org/10.1016/bs.mie.2018.08.026

APA

Prestel, A., Bugge, K., Staby, L., Hendus-Altenburger, R., & Kragelund, B. B. (2018). Characterization of Dynamic IDP Complexes by NMR Spectroscopy. I E. Rhoades (red.), Intrinsically Disordered Proteins (s. 193-226). Academic Press. Methods in Enzymology Bind 611 https://doi.org/10.1016/bs.mie.2018.08.026

Vancouver

Prestel A, Bugge K, Staby L, Hendus-Altenburger R, Kragelund BB. Characterization of Dynamic IDP Complexes by NMR Spectroscopy. I Rhoades E, red., Intrinsically Disordered Proteins. Academic Press. 2018. s. 193-226. (Methods in Enzymology, Bind 611). https://doi.org/10.1016/bs.mie.2018.08.026

Author

Prestel, Andreas ; Bugge, Katrine ; Staby, Lasse ; Hendus-Altenburger, Ruth ; Kragelund, Birthe B. / Characterization of Dynamic IDP Complexes by NMR Spectroscopy. Intrinsically Disordered Proteins. red. / Elizabeth Rhoades. Academic Press, 2018. s. 193-226 (Methods in Enzymology, Bind 611).

Bibtex

@inbook{b2ca753fb93a482e8280f05010434846,
title = "Characterization of Dynamic IDP Complexes by NMR Spectroscopy",
abstract = "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.",
keywords = "Affinity, Dynamics, Fuzzy, Integrative structural biology, Interaction, Intrinsically disordered proteins, Ligand binding, Practical sample preparation, Protein",
author = "Andreas Prestel and Katrine Bugge and Lasse Staby and Ruth Hendus-Altenburger and Kragelund, {Birthe B.}",
year = "2018",
doi = "10.1016/bs.mie.2018.08.026",
language = "English",
isbn = "978-0-12-815649-0",
series = "Methods in Enzymology",
publisher = "Academic Press",
pages = "193--226",
editor = "Elizabeth Rhoades",
booktitle = "Intrinsically Disordered Proteins",
address = "United States",

}

RIS

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