[NMR paper] Production of human A2AAR in lipid nanodiscs for 19F-NMR and single-molecule fluorescence spectroscopy
Production of human A2AAR in lipid nanodiscs for 19F-NMR and single-molecule fluorescence spectroscopy
We describe production of the human A(2A) adenosine receptor (A(2A)AR), a class A G protein-coupled receptor (GPCR) for ^(19)F-NMR and single-molecule fluorescence (SMF) spectroscopy. We explain in detail steps shared between the two sample preparation strategies, including expression and isolation of A(2A)AR and assembly of A(2A)AR in lipid nanodiscs and procedures for incorporation of either ^(19)F-NMR or fluorescence probes. Protocols for SMF experiments include sample setup, data...
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07-17-2022 10:07 PM
[NMR paper] Synergies of Single Molecule Fluorescence and NMR for the Study of Intrinsically Disordered Proteins
Synergies of Single Molecule Fluorescence and NMR for the Study of Intrinsically Disordered Proteins
Single molecule fluorescence and nuclear magnetic resonance spectroscopy (NMR) are two very powerful techniques for the analysis of intrinsically disordered proteins (IDPs). Both techniques have individually made major contributions to deciphering the complex properties of IDPs and their interactions, and it has become evident that they can provide very complementary views on the distance-dynamics relationships of IDP systems. We now review the first approaches using both NMR and single...
[NMR paper] Single-Molecule Force Spectroscopy Trajectories of a Single Protein and Its Polyproteins Are Equivalent: A Direct Experimental Validation Based on A Small Protein NuG2
Single-Molecule Force Spectroscopy Trajectories of a Single Protein and Its Polyproteins Are Equivalent: A Direct Experimental Validation Based on A Small Protein NuG2
Single-molecule force spectroscopy (SMFS) has become a powerful tool in investigating the mechanical unfolding/folding of proteins at the single-molecule level. Polyproteins made of tandem identical repeats have been widely used in atomic force microscopy (AFM)-based SMFS studies, where polyproteins not only serve as fingerprints to identify single-molecule stretching events, but may also improve statistics of data...
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12-27-2016 11:04 PM
[NMR paper] Gradual Disordering of the Native State on a Slow Two-State Folding Protein Monitored by Single-Molecule Fluorescence Spectroscopy and NMR.
Gradual Disordering of the Native State on a Slow Two-State Folding Protein Monitored by Single-Molecule Fluorescence Spectroscopy and NMR.
Gradual Disordering of the Native State on a Slow Two-State Folding Protein Monitored by Single-Molecule Fluorescence Spectroscopy and NMR.
J Phys Chem B. 2013 Jun 24;
Authors: Campos LA, Sadqi M, Liu J, Wang X, English DS, Munoz V
Abstract
Theory predicts that folding free energy landscapes are intrinsically malleable, and as such are expected to respond to perturbations in topographically complex...
[NMR paper] (13)C-(1)H NMR relaxation and fluorescence anisotropy decay study of tyrosine dynamic
(13)C-(1)H NMR relaxation and fluorescence anisotropy decay study of tyrosine dynamics in motilin.
Related Articles (13)C-(1)H NMR relaxation and fluorescence anisotropy decay study of tyrosine dynamics in motilin.
Biophys J. 2002 Nov;83(5):2812-25
Authors: Damberg P, Jarvet J, Allard P, Mets U, Rigler R, Gräslund A
Tyrosine ring dynamics of the gastrointestinal hormone motilin was studied using two independent physical methods: fluorescence polarization anisotropy decay and NMR relaxation. Motilin, a 22-residue peptide, was selectively (13)C...
Nuclear magnetic resonance/single molecule fluorescence combinations to study dynamic protein systems - ScienceDirect
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