(Q58045305)

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Fractional 13C enrichment of isolated carbons using [1-13C]- or [2-13C]-glucose facilitates the accurate measurement of dynamics at backbone Cα and side-chain methyl positions in proteins

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scholarly article

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Fractional 13C enrichment of isolated carbons using [1-13C]- or [2-13C]-glucose facilitates the accurate measurement of dynamics at backbone Cα and side-chain methyl positions in proteins (English)

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object named as

Silke Wiesner

5

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object named as

Kaare Teilum

2

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9

object named as

Lewis E. Kay

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author name string

Patrik Lundström

1

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Tommy Carstensen

3

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Irina Bezsonova

4

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D. Flemming Hansen

6

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Tomasz L. Religa

7

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Mikael Akke

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publication date

7 June 2007

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Journal of Biomolecular NMR

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38

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3

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199-212

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https://scigraph.springernature.com/pub.10.1007/s10858-007-9158-6

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Gene synthesis, expression in Escherichia coli, purification and characterization of the recombinant bovine acyl-CoA-binding protein

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Temperature dependence of anisotropic protein backbone dynamics

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https://pubmed.ncbi.nlm.nih.gov/17554498

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Carbon relaxation in randomly fractionally 13C-enriched proteins

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Measurement of (13)C (α)- (13)CO cross-relaxation rates in (15)N-/ (13)C-labelled proteins

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Carbonyl carbon transverse relaxation dispersion measurements and ms-micros timescale motion in a protein hydrogen bond network

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Disulfide Bond Isomerization in Basic Pancreatic Trypsin Inhibitor: Multisite Chemical Exchange Quantified by CPMG Relaxation Dispersion and Chemical Shift Modeling

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Two-dimensional 1H NMR study of human ubiquitin: a main chain directed assignment and structure analysis.

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Study of protein dynamics in solution by measurement of (13)C (α)- (13)CO NOE and (13)CO longitudinal relaxation

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Improved labeling strategy for 13C relaxation measurements of methyl groups in proteins.

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Biosynthetic 13C labeling of aromatic side chains in proteins for NMR relaxation measurements

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Dynamics of methyl groups in proteins as studied by proton-detected 13C NMR spectroscopy. Application to the leucine residues of staphylococcal nuclease

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Slow internal dynamics in proteins: application of NMR relaxation dispersion spectroscopy to methyl groups in a cavity mutant of T4 lysozyme

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Functional dynamics of human FKBP12 revealed by methyl 13C rotating frame relaxation dispersion NMR spectroscopy

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A single-quantum methyl 13C-relaxation dispersion experiment with improved sensitivity

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Investigation of protein motions via relaxation measurements

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Slow dynamics in folded and unfolded states of an SH3 domain

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The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

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Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease

1 reference

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Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: application to methionine residues in a cavity mutant of T4 lysozyme

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New tools provide new insights in NMR studies of protein dynamics

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NMR characterization of the dynamics of biomacromolecules

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Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules

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An 15N NMR spin relaxation dispersion study of the folding of a pair of engineered mutants of apocytochrome b562.

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Studying excited states of proteins by NMR spectroscopy.

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Cross-correlated chemical shift modulation: a signature of slow internal motions in proteins.

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Optimized labeling of 13CHD2 methyl isotopomers in perdeuterated proteins: potential advantages for 13C relaxation studies of methyl dynamics of larger proteins

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1 reference

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10.1007/S10858-007-9158-6

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