Related ArticlesNMR Lineshape Analysis of Intrinsically Disordered Protein Interactions.
Methods Mol Biol. 2020;2141:477-504
Authors: Waudby CA, Christodoulou J
Abstract
Interactions of intrinsically disordered proteins are central to their cellular functions, and solution-state NMR spectroscopy provides a powerful tool for characterizing both structural and mechanistic aspects of such interactions. Here we focus on the analysis of IDP interactions using NMR titration measurements. Changes in resonance lineshapes in two-dimensional NMR spectra upon titration with a ligand contain rich information on structural changes in the protein and the thermodynamics and kinetics of the interaction, as well as on the microscopic association mechanism. Here we present protocols for the optimal design of titration experiments, data acquisition, and data analysis by two-dimensional lineshape fitting using the TITAN software package.
[NMR paper] Rapid Quantification of Protein-Ligand Binding via 19F NMR Lineshape Analysis.
Rapid Quantification of Protein-Ligand Binding via 19F NMR Lineshape Analysis.
Related Articles Rapid Quantification of Protein-Ligand Binding via 19F NMR Lineshape Analysis.
Biophys J. 2020 Apr 15;:
Authors: Stadmiller SS, Aguilar JS, Waudby CA, Pielak GJ
Abstract
Fluorine incorporation is ideally suited to many NMR techniques, and incorporation of fluorine into proteins and fragment libraries for drug discovery has become increasingly common. Here, we use one-dimensional 19F NMR lineshape analysis to quantify the kinetics and...
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[NMR paper] Direct Detection of Carbon and Nitrogen Nuclei for High-Resolution Analysis of Intrinsically Disordered Proteins using NMR Spectroscopy.
Direct Detection of Carbon and Nitrogen Nuclei for High-Resolution Analysis of Intrinsically Disordered Proteins using NMR Spectroscopy.
Direct Detection of Carbon and Nitrogen Nuclei for High-Resolution Analysis of Intrinsically Disordered Proteins using NMR Spectroscopy.
Methods. 2018 Jan 13;:
Authors: Gibbs EB, Kriwacki RW
Abstract
Nuclear magnetic resonance spectroscopy (NMR) is a powerful technique for characterizing the structural and dynamic properties of intrinsically disordered proteins and protein regions (IDPs &...
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01-18-2018 12:41 PM
Direct Detection of Carbon and Nitrogen Nuclei for High-Resolution Analysis of Intrinsically Disordered Proteins using NMR Spectroscopy
Direct Detection of Carbon and Nitrogen Nuclei for High-Resolution Analysis of Intrinsically Disordered Proteins using NMR Spectroscopy
Publication date: Available online 16 January 2018
Source:Methods</br>
Author(s): E.B. Gibbs, R.W. Kriwacki</br>
Nuclear magnetic resonance spectroscopy (NMR) is a powerful technique for characterizing the structural and dynamic properties of intrinsically disordered proteins and protein regions (IDPs & IDRs). However, the application of NMR to IDPs has been limited by poor chemical shift dispersion in two-dimensional (2D) 1H-15N...
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01-17-2018 07:00 PM
[NMR paper] Common molecular pathogenesis of disease-related intrinsically disordered proteins revealed by NMR analysis.
Common molecular pathogenesis of disease-related intrinsically disordered proteins revealed by NMR analysis.
Common molecular pathogenesis of disease-related intrinsically disordered proteins revealed by NMR analysis.
J Biochem. 2017 Sep 11;:
Authors: Shigemitsu Y, Hiroaki H
Abstract
Intrinsically disordered proteins (IDPs) are either completely unstructured or contain large disordered regions in their native state; they have drawn much attention in the field of molecular pathology. Some of them substantially tend to form...
[NMR paper] Tyrosine Phosphorylation within the Intrinsically Disordered Cytosolic Domains of the B-Cell Receptor: An NMR-Based Structural Analysis.
Tyrosine Phosphorylation within the Intrinsically Disordered Cytosolic Domains of the B-Cell Receptor: An NMR-Based Structural Analysis.
Related Articles Tyrosine Phosphorylation within the Intrinsically Disordered Cytosolic Domains of the B-Cell Receptor: An NMR-Based Structural Analysis.
PLoS One. 2014;9(4):e96199
Authors: Rosenlöw J, Isaksson L, Mayzel M, Lengqvist J, Orekhov VY
Abstract
Intrinsically disordered proteins are found extensively in cell signaling pathways where they often are targets of posttranslational...
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04-29-2014 12:04 PM
4D Non-uniformly sampled HCBCACON and 1J(NCα)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins
4D Non-uniformly sampled HCBCACON and 1J(NCα)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins
Abstract A pair of 4D NMR experiments for the backbone assignment of disordered proteins is presented. The experiments exploit 13C direct detection and non-uniform sampling of the indirectly detected dimensions, and provide correlations of the aliphatic proton (Hα, and Hβ) and carbon (Cα, Cβ) resonance frequencies to the protein backbone. Thus, all the chemical shifts regularly used to map the transient...
NMR Lineshape Analysis of Intrinsically Disordered Protein Interactions.
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