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Sedimentation of large, soluble proteins up to 140 kDa for 1H-detected MAS NMR and 13C DNP NMR – practical aspects
Sedimentation of large, soluble proteins up to 140 kDa for 1H-detected MAS NMR and 13C DNP NMR – practical aspects
Solution NMR is typically applied to biological systems with molecular weights < 40 kDa wherea...
Decorating phenylalanine side-chains with triple labeled 13C/19F/2H isotope patterns
Decorating phenylalanine side-chains with triple labeled 13C/19F/2H isotope patterns
We present an economic and straightforward method to introduce 13C-19F spin systems into the deuterated aromatic side chai...
Micromolar fluoride contamination arising from glass NMR tubes and a simple solution for biomolecular applications
Micromolar fluoride contamination arising from glass NMR tubes and a simple solution for biomolecular applications
Fluorine (19F) NMR is emerging as an invaluable analytical technique in chemistry, biochemistry, structural biology, mater...
Deuterium spin relaxation of fractionally deuterated ribonuclease H using paired 475 and 950 MHz NMR spectrometers
Deuterium spin relaxation of fractionally deuterated ribonuclease H using paired 475 and 950 MHz NMR spectrometers
Deuterium (2H) spin relaxation of 13CH2D methyl groups has been widely applied to investigate picosecond-to-nanosecond con...
Quantitative analysis of the slow exchange process by 19F NMR in the presence of scalar and dipolar couplings: applications to the ribose 2′-19F probe in nucleic acids
Quantitative analysis of the slow exchange process by 19F NMR in the presence of scalar and dipolar couplings: applications to the ribose 2′-19F probe in nucleic acids
Solution NMR spectroscopy is a particularly powerful technique for characterizing the functional dynamics of biomolecules,...
Towards cost-effective side-chain isotope labelling of proteins expressed in human cells
Towards cost-effective side-chain isotope labelling of proteins expressed in human cells
Side chain isotope labelling is a powerful tool to study protein structure and interactions by NMR spectroscopy. 1H,13C la...
Transverse relaxation optimized spectroscopy of NH2 groups in glutamine and asparagine side chains of proteins
Transverse relaxation optimized spectroscopy of NH2 groups in glutamine and asparagine side chains of proteins
A transverse relaxation optimized spectroscopy (TROSY) approach is described for the optimal detection of NH2 groups in as...
Optimising in-cell NMR acquisition for nucleic acids
Optimising in-cell NMR acquisition for nucleic acids
Understanding the structure and function of nucleic acids in their native environment is crucial to structural biology and...
19F NMR relaxation of buried tryptophan side chains suggest anisotropic rotational diffusion of the protein RfaH
19F NMR relaxation of buried tryptophan side chains suggest anisotropic rotational diffusion of the protein RfaH
The recent application of 19F NMR in the study of biomolecular structure and dynamics has made it a potentially attractive...
Reducing experimental time through spin-lattice relaxation enhancement via dissolved oxygen
Reducing experimental time through spin-lattice relaxation enhancement via dissolved oxygen
Large proteins and dilute spin systems within a deuterated background are often characterized by long proton (1H) spin-lat...
Local structure propensities in disordered proteins from cross-correlated NMR spin relaxation
Local structure propensities in disordered proteins from cross-correlated NMR spin relaxation
Structurally diverse ensembles of intrinsically disordered proteins or regions are difficult to determine, because experim...
Pitfalls in measurements of R1 relaxation rates of protein backbone 15N nuclei
Pitfalls in measurements of R1 relaxation rates of protein backbone 15N nuclei
The dynamics of the backbone and side-chains of protein are routinely studied by interpreting experimentally determined 15...
Counterintuitive method improves yields of isotopically labelled proteins expressed in flask-cultured Escherichia coli
Counterintuitive method improves yields of isotopically labelled proteins expressed in flask-cultured Escherichia coli
NMR is a powerful tool for the structural and dynamic study of proteins. One of the necessary conditions for the study of ...
Alpha-helices as alignment reporters in residual dipolar coupling analysis of proteins
Alpha-helices as alignment reporters in residual dipolar coupling analysis of proteins
Inclusion of residual dipolar couplings (RDCs) during the early rounds of protein structure determination requires use of ...
Using temperature coefficients to support resonance assignment of intrinsically disordered proteins
Using temperature coefficients to support resonance assignment of intrinsically disordered proteins
The resonance assignment of large intrinsically disordered proteins (IDPs) is difficult due to the low dispersion of chemi...
Evaluation of TOCSY mixing for sensitivity-enhancement in solid-state NMR and application of 4D experiments for side-chain assignments of the full-length 30 kDa membrane protein GlpG
Evaluation of TOCSY mixing for sensitivity-enhancement in solid-state NMR and application of 4D experiments for side-chain assignments of the full-length 30 kDa membrane protein GlpG
Chemical shift assignments of large membrane proteins by solid-state NMR experiments are challenging. Recent advancements ...
15N-detected TROSY for 1H-15N heteronuclear correlation to study intrinsically disordered proteins: strategies to increase spectral quality
15N-detected TROSY for 1H-15N heteronuclear correlation to study intrinsically disordered proteins: strategies to increase spectral quality
Intrinsically disordered proteins and protein regions are central to many biological processes but difficult to characteri...
Solid state NMR spectral editing of histidine, arginine and lysine using Hadamard encoding
Solid state NMR spectral editing of histidine, arginine and lysine using Hadamard encoding
The NMR signals from protein sidechains are rich in information about intra- and inter-molecular interactions, but their d...
19F-NMR studies of the impact of different detergents and nanodiscs on the A2A adenosine receptor
19F-NMR studies of the impact of different detergents and nanodiscs on the A2A adenosine receptor
For the A2A adenosine receptor (A2AAR), a class A G-protein-coupled receptor (GPCR), reconstituted in n-dodecyl-β-D-m...
Uniform [13C,15N]-labeled and glycosylated IgG1 Fc expressed in Saccharomyces cerevisiae
Uniform [13C,15N]-labeled and glycosylated IgG1 Fc expressed in Saccharomyces cerevisiae
Despite the prevalence and importance of glycoproteins in human biology, methods for isotope labeling suffer significant l...
5D solid-state NMR spectroscopy for facilitated resonance assignment
5D solid-state NMR spectroscopy for facilitated resonance assignment
1H-detected solid-state NMR spectroscopy has been becoming increasingly popular for the characterization of protein struct...
Efficient determination of the accessible conformation space of multi-domain complexes based on EPR PELDOR data
Efficient determination of the accessible conformation space of multi-domain complexes based on EPR PELDOR data
Many proteins can adopt multiple conformations which are important for their function. This is also true for proteins and ...
Paramagnetic NMR to study iron sulfur proteins: 13C detected experiments illuminate the vicinity of the metal center
Paramagnetic NMR to study iron sulfur proteins: 13C detected experiments illuminate the vicinity of the metal center
The robustness of NMR coherence transfer in proximity of a paramagnetic center depends on the relaxation properties of the...
Synthesis of a 13C-methylene-labeled isoleucine precursor as a useful tool for studying protein side-chain interactions and dynamics
Synthesis of a 13C-methylene-labeled isoleucine precursor as a useful tool for studying protein side-chain interactions and dynamics
In this study, we present the synthesis and incorporation of a metabolic isoleucine precursor compound for selective methy...
Breaking boundaries: TINTO in POKY for computer vision-based NMR walking strategies
Breaking boundaries: TINTO in POKY for computer vision-based NMR walking strategies
Nuclear magnetic resonance is a crucial technique for studying biological complexes, as it provides precise structural and...
A thermosensitive gel matrix for bioreactor-assisted in-cell NMR of nucleic acids and proteins
A thermosensitive gel matrix for bioreactor-assisted in-cell NMR of nucleic acids and proteins
Introducing the flow through the bioreactor has revolutionized in-cell NMR spectroscopy by prolonging the measurement time...
Strategies for acquisition of resonance assignment spectra of highly dynamic membrane proteins: a GPCR case study
Strategies for acquisition of resonance assignment spectra of highly dynamic membrane proteins: a GPCR case study
In protein nuclear magnetic resonance (NMR), chemical shift assignment provides a wealth of information. However, acquisit...
Improved spectral resolution of [13C,1H]-HSQC spectra of aromatic amino acid residues in proteins produced by cell-free synthesis from inexpensive 13C-labelled precursors
Improved spectral resolution of [13C,1H]-HSQC spectra of aromatic amino acid residues in proteins produced by cell-free synthesis from inexpensive 13C-labelled precursors
Cell-free protein synthesis using eCells allows production of amino acids from inexpensive 13C-labelled precursors. We sho...
Studying micro to millisecond protein dynamics using simple amide 15N CEST experiments supplemented with major-state R2 and visible peak-position constraints
Studying micro to millisecond protein dynamics using simple amide 15N CEST experiments supplemented with major-state R2 and visible peak-position constraints
Over the last decade amide 15N CEST experiments have emerged as a popular tool to study protein dynamics that involves exc...
E. coli “Stablelabel” S30 lysate for optimized cell-free NMR sample preparation
E. coli “Stablelabel” S30 lysate for optimized cell-free NMR sample preparation
Cell-free (CF) synthesis with highly productive E. coli lysates is a convenient method to produce labeled proteins for NMR...
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