NMR Spectroscopic Studies of the Conformational Ensembles of Intrinsically Disordered Proteins View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2015

AUTHORS

Dennis Kurzbach , Georg Kontaxis , Nicolas Coudevylle , Robert Konrat

ABSTRACT

Intrinsically disordered proteins (IDPs) are characterized by substantial conformational flexibility and thus not amenable to conventional structural biology techniques. Given their inherent structural flexibility NMR spectroscopy offers unique opportunities for structural and dynamic studies of IDPs. The past two decades have witnessed significant development of NMR spectroscopy that couples advances in spin physics and chemistry with a broad range of applications. This chapter will summarize key advances in NMR methodology. Despite the availability of efficient (multi-dimensional) NMR experiments for signal assignment of IDPs it is discussed that NMR of larger and more complex IDPs demands spectral simplification strategies capitalizing on specific isotope-labeling strategies. Prototypical applications of isotope labeling-strategies are described. Since IDP-ligand association and dissociation processes frequently occur on time scales that are amenable to NMR spectroscopy we describe in detail the application of CPMG relaxation dispersion techniques to studies of IDP protein binding. Finally, we demonstrate that the complementary usage of NMR and EPR data provide a more comprehensive picture about the conformational states of IDPs and can be employed to analyze the conformational ensembles of IDPs. More... »

PAGES

149-85

References to SciGraph publications

Book

TITLE

Intrinsically Disordered Proteins Studied by NMR Spectroscopy

ISBN

978-3-319-20163-4
978-3-319-20164-1

Author Affiliations

From Grant

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-3-319-20164-1_5

DOI

http://dx.doi.org/10.1007/978-3-319-20164-1_5

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1030841784

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/26387102


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