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Nature, ISSN 0028-0836, 12/2011, Volume 480, Issue 7376, pp. 268 - 272
Journal Article
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 06/2019, Volume 141, Issue 22, pp. 9004 - 9017
Although the α-helix has long been recognized as an all-important element of secondary structure, it generally requires stabilization by tertiary interactions... 
Journal Article
Journal of Biomolecular NMR, ISSN 0925-2738, 11/2009, Volume 45, Issue 3, p. 241
A shift of the water proton precession frequency is described that can introduce errors in chemical shifts derived using the water signal as the chemical shift... 
Radiation | Detectors
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 07/2010, Volume 132, Issue 29, pp. 9948 - 9951
Journal Article
Journal of Biomolecular NMR, ISSN 0925-2738, 2009, Volume 45, Issue 3, pp. 241 - 244
A shift of the water proton precession frequency is described that can introduce errors in chemical shifts derived using the water signal as the chemical shift... 
Water | Chemical shift | Precession | Reference | Proton | Frequency | Probe | Tuning | Protons | Nuclear Magnetic Resonance, Biomolecular - methods | Water - chemistry
Journal Article
Journal of Magnetic Resonance, ISSN 1090-7807, 07/2016, Volume 268, p. 73
Display Omitted 
Journal Article
Journal of Magnetic Resonance, ISSN 1090-7807, 07/2016, Volume 268, p. 73
To access, purchase, authenticate, or subscribe to the full-text of this article, please visit this link: http://dx.doi.org/10.1016/j.jmr.2016.05.001 A new and... 
Measurement | Proteins | Proteases | Analysis | Glycine
Journal Article
Journal of Magnetic Resonance, ISSN 1090-7807, 07/2016, Volume 268, pp. 73 - 81
A new and convenient method, named ARTSY-J, is introduced that permits extraction of the super(3)J sub(HNH alpha ) couplings in proteins from the relative... 
Proteins | Couplings | Residues | Mathematical analysis | Mathematical models | Spectra | Cross relaxation | Delay
Journal Article
Journal of Magnetic Resonance, ISSN 1090-7807, 07/2016, Volume 268, pp. 73 - 81
A new and convenient method, named ARTSY-J, is introduced that permits extraction of the couplings in proteins from the relative intensities in a pair of N– H... 
TROSY | Karplus equation | Gly | Protein NMR | HIV-1 Protease | GB3 | Backbone torsion angle | protein NMR | backbone torsion angle
Journal Article
Nature Protocols, ISSN 1754-2189, 08/2012, Volume 7, Issue 8, pp. 1523 - 1533
We present the protocol for the measurement and analysis of dark-state exchange saturation transfer (DEST), a novel solution NMR method for characterizing, at... 
RELAXATION | BIOCHEMICAL RESEARCH METHODS | Macromolecular Substances - chemistry | Molecular Weight | Time Factors | Nuclear Magnetic Resonance, Biomolecular - methods | Software | Amyloid beta-Peptides - chemistry | Kinetics | Nitrogen Isotopes | Physiological aspects | Nuclear magnetic resonance spectroscopy | Usage | Research | Amyloid beta-protein
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 08/2017, Volume 139, Issue 32, pp. 11036 - 11039
A method is introduced that permits direct observation of the rates at which backbone amide hydrogens become protected from solvent exchange after rapidly... 
BETA-HAIRPIN | RIBONUCLEASE-A | MECHANISM | PATHWAY | UBIQUITIN | DYNAMICS | STATE | DENATURATION | STAPHYLOCOCCAL NUCLEASE | CHEMISTRY, MULTIDISCIPLINARY | INSIGHTS | Ubiquitin | Nuclear magnetic resonance spectroscopy | Usage | Research | Isostatic pressing
Journal Article
Protein Science, ISSN 0961-8368, 03/2011, Volume 20, Issue 3, pp. 500 - 512
Journal Article
The Journal of Physical Chemistry B, ISSN 1520-6106, 05/2008, Volume 112, Issue 19, pp. 6045 - 6056
Journal Article
Protein Science, ISSN 0961-8368, 09/2011, Volume 20, Issue 9, p. 1643
Journal Article
Journal of Biomolecular NMR, ISSN 0925-2738, 6/2004, Volume 29, Issue 2, pp. 187 - 198
A constant-time, Carr–Purcell–Meiboom–Gill (CPMG) transverse relaxation, R2, dispersion experiment for carbonyl carbons was designed and executed to detect... 
Polymer Sciences | Chemistry | NMR | R 2 | CPMG | conformational change | Animal Anatomy / Morphology / Histology | chemical exchange | R | Chemical exchange | Conformational change
Journal Article
Nature, ISSN 0028-0836, 02/2007, Volume 445, Issue 7128, pp. 609 - 609
Nuclear magnetic resonance is the best way to study motion in proteins, but it could be applied only to small systems. This limitation has been overcome to... 
Journal Article