The use of protein building blocks for the structure determination of multidomain proteins and proteinâ??protein complexes, also known as the â??divide and conquerâ?? approach, is an important strategy for obtaining protein structures. Atomic-resolution X-ray or NMR data of the individual domains are combined with lower-resolution electron microscopy maps or X-ray data of the full-length protein or the protein complex. Doing so, it is often assumed that the individual domain structures remain invariant in the context of the superstructure. In this work, we show the potentials and limitations of NMR to validate this approach at the example of the dodecameric DnaB helicase from Helicobacter pylori. We investigate how sequentially assigned spectra, as well as unassigned spectral fingerprints can be used to indicate the conservation of individual domains, and also to highlight conformational differences.
[NMR paper] NMR approaches for structural analysis of multidomain proteins and complexes in solution.
NMR approaches for structural analysis of multidomain proteins and complexes in solution.
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Prog Nucl Magn Reson Spectrosc. 2014 Jul;80C:26-63
Authors: Göbl C, Madl T, Simon B, Sattler M
Abstract
NMR spectroscopy is a key method for studying the structure and dynamics of (large) multidomain proteins and complexes in solution. It plays a unique role in integrated structural biology approaches as especially information about...
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NMR approaches for structural analysis of multidomain proteins and complexes in solution
NMR approaches for structural analysis of multidomain proteins and complexes in solution
Publication date: Available online 23 May 2014
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Christoph Göbl , Tobias Madl , Bernd Simon , Michael Sattler</br>
NMR spectroscopy is a key method for studying the structure and dynamics of (large) multidomain proteins and complexes in solution. It plays a unique role in integrated structural biology approaches as especially information about conformational dynamics can be readily obtained at residue...
[NMR paper] NMR structural comparison of the cytoplasmic juxtamembrane domains of G-protein-coupl
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Authors: Xie XQ, Chen JZ
The fourth cytoplasmic domain, the so-called C-terminal juxtamembrane segment or helix VIII, has been identified in numerous G-protein-coupled...
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[NMR paper] Leveraging structural approaches: applications of NMR-based screening and X-ray cryst
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J Synchrotron Radiat. 2004 Jan 1;11(Pt 1):97-100
Authors: Moore J, Abdul-Manan N, Fejzo J, Jacobs M, Lepre C, Peng J, Xie X
In the last several years, NMR strategies in drug discovery have evolved from a primarily structural focus to a set of technologies that are non-structural in nature but...
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[NMR paper] Structural rearrangements of the two domains of Azotobacter vinelandii rhodanese upon
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Int J Biol Macromol. 2003 Dec;33(4-5):193-201
Authors: Cicero DO, Melino S, Orsale M, Brancato G, Amadei A,...
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[NMR paper] Structural consequences of site-directed mutagenesis in flexible protein domains: NMR
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Eur J Biochem. 2001 Apr;268(8):2253-60
Authors: Golovanov AP, Hawkins D, Barsukov I, Badii R, Bokoch GM, Lian LY, Roberts GC
The guanine dissociation inhibitor RhoGDI consists of a folded C-terminal domain and a highly flexible N-terminal region, both of...
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[NMR paper] NMR analysis of cbEGF domains gives new insights into the structural consequences of
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Protein Eng. 1998 Nov;11(11):957-9
Authors: Whiteman P, Downing AK, Handford PA
Fibrillin-1 is a modular glycoprotein and a major component of the 10-12 nm microfibrils of the extracellular matrix. Mutations in the fibrillin-1 (FBN 1) gene result in the connective tissue disease the...