Publication date: Available online 27 April 2018 Source:Methods
Author(s): Katarzyna Grudzi??, Anna Zawadzka-Kazimierczuk, Wiktor Ko?mi?ski
Intrinsically disordered proteins (IDPs) are getting more and more interest of the scientific community. Nuclear magnetic resonance (NMR) is often a technique of choice for these studies, as it provides atomic-resolution information on structure, dynamics and interactions of IDPs. Nonetheless, NMR spectra of IDPs are typically extraordinary crowded, comparing to those of structured proteins. To overcome this problem, high-dimensional NMR experiments can be used, which allow for a better peak separation. In the present review different aspects of such experiments are discussed, from data acquisition and processing to analysis, focusing on experiments for resonance assignment.
[NMR paper] Application of NMR to studies of intrinsically disordered proteins.
Application of NMR to studies of intrinsically disordered proteins.
Related Articles Application of NMR to studies of intrinsically disordered proteins.
Arch Biochem Biophys. 2017 May 11;:
Authors: Gibbs EB, Cook EC, Showalter SA
Abstract
The prevalence of intrinsically disordered protein regions, particularly in eukaryotic proteins, and their clear functional advantages for signaling and gene regulation have created an imperative for high-resolution structural and mechanistic studies. NMR spectroscopy has played a central role...
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05-16-2017 10:27 PM
A six-dimensional alpha proton detection-based APSY experiment for backbone assignment of intrinsically disordered proteins
A six-dimensional alpha proton detection-based APSY experiment for backbone assignment of intrinsically disordered proteins
Abstract
Sequence specific resonance assignment is the prerequisite for the NMR-based analysis of the conformational ensembles and their underlying dynamics of intrinsically disordered proteins. However, rapid solvent exchange in intrinsically disordered proteins often complicates assignment strategies based on HN-detection. Here we present a six-dimensional alpha proton detection-based automated projection spectroscopy (APSY)...
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11-04-2014 01:02 AM
[NMR paper] Novel methods based on 13C detection to study intrinsically disordered proteins
Novel methods based on 13C detection to study intrinsically disordered proteins
Publication date: April 2014
Source:Journal of Magnetic Resonance, Volume 241</br>
Author(s): Isabella C. Felli , Roberta Pierattelli</br>
Intrinsically disordered proteins (IDPs) are characterized by highly flexible solvent exposed backbones and can sample many different conformations. These properties confer them functional advantages, complementary to those of folded proteins, which need to be characterized to expand our view of how protein structural and dynamic features affect...
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03-22-2014 01:28 AM
[NMR paper] Enhancing the resolution of multi-dimensional heteronuclear NMR spectra of intrinsically disordered proteins by homonuclear broadband decoupling.
Enhancing the resolution of multi-dimensional heteronuclear NMR spectra of intrinsically disordered proteins by homonuclear broadband decoupling.
Related Articles Enhancing the resolution of multi-dimensional heteronuclear NMR spectra of intrinsically disordered proteins by homonuclear broadband decoupling.
Chem Commun (Camb). 2013 Dec 23;
Authors: Helge Meyer N, Zangger K
Abstract
Limited spectral resolution in the proton dimension of NMR spectra is a severe problem in intrinsically disordered proteins. Here we show that homonuclear...
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12-25-2013 03:39 PM
[NMR paper] Generating NMR Chemical Shift Assignments of Intrinsically Disordered Proteins Using Carbon-Detect NMR Methods.
Generating NMR Chemical Shift Assignments of Intrinsically Disordered Proteins Using Carbon-Detect NMR Methods.
Related Articles Generating NMR Chemical Shift Assignments of Intrinsically Disordered Proteins Using Carbon-Detect NMR Methods.
Anal Biochem. 2013 Dec 9;
Authors: Sahu D, Bastidas M, Showalter S
Abstract
There is an extraordinary need to describe the structures of intrinsically disordered proteins (IDPs) due to their role in various biological processes involved in signaling and transcription. However, general study of IDPs...
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12-18-2013 04:00 PM
Generating NMR Chemical Shift Assignments of Intrinsically Disordered Proteins Using Carbon-Detect NMR Methods
Generating NMR Chemical Shift Assignments of Intrinsically Disordered Proteins Using Carbon-Detect NMR Methods
Publication date: Available online 10 December 2013
Source:Analytical Biochemistry</br>
Author(s): Debashish Sahu , Monique Bastidas , Scott Showalter</br>
There is an extraordinary need to describe the structures of intrinsically disordered proteins (IDPs) due to their role in various biological processes involved in signaling and transcription. However, general study of IDPs by NMR spectroscopy is limited by the poor 1H-amide chemical shift dispersion...
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12-10-2013 04:48 AM
High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins
High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins
Abstract Four novel 5D (HACA(N)CONH, HNCOCACB, (HACA)CON(CA)CONH, (H)NCO(NCA)CONH), and one 6D ((H)NCO(N)CACONH) NMR pulse sequences are proposed. The new experiments employ non-uniform sampling that enables achieving high resolution in indirectly detected dimensions. The experiments facilitate resonance assignment of intrinsically disordered proteins. The novel pulse sequences were successfully tested using δ subunit (20 kDa) of Bacillus subtilis RNA polymerase...
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02-21-2012 03:40 AM
Paramagnetic relaxation enhancement to improve sensitivity of fast NMR methods: application to intrinsically disordered proteins
Paramagnetic relaxation enhancement to improve sensitivity of fast NMR methods: application to intrinsically disordered proteins
Abstract We report enhanced sensitivity NMR measurements of intrinsically disordered proteins in the presence of paramagnetic relaxation enhancement (PRE) agents such as Ni2+-chelated DO2A. In proton-detected 1H-15N SOFAST-HMQC and carbon-detected (H-flip)13CO-15N experiments, faster longitudinal relaxation enables the usage of even shorter interscan delays. This results in higher NMR signal intensities per units of experimental time, without adverse line...
High-dimensional NMR methods for intrinsically disordered proteins studies
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