Journal ArticleDOI
Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins
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This article is published in Journal of the American Chemical Society.The article was published on 1990-06-01. It has received 1028 citations till now. The article focuses on the topics: Relaxation (NMR).read more
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Backbone Dynamics of a Free and a Phosphopeptide-Complexed Src Homology 2 Domain Studied by 15N NMR Relaxation
Neil A. Farrow,Ranjith Muhandiram,Alex U. Singer,Steven M. Pascal,Cyril M. Kay,Gerry Gish,Steven E. Shoelson,Tony Pawson,Julie D. Forman-Kay,Lewis E. Kay +9 more
TL;DR: Overall, higher order parameters were not found in the peptide-bound form, indicating that on average, picosecond-time-scale disorder is not reduced upon binding peptide, and the relaxation data of the SH2-phosphopeptide complex were fit with fewer exchange terms than the uncomplexed form.
Journal ArticleDOI
Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible.
TL;DR: The backbone dynamics of Ca(2+)-saturated recombinant Drosophila calmodulin has been studied by 15N longitudinal and transverse relaxation experiments, combined with 15N(1H) NOE measurements, showing a high degree of mobility near the middle of the central helix and anisotropy observed in the motion of the two globular cal modulin domains is much smaller than expected.
Journal ArticleDOI
Two-state allosteric behavior in a single-domain signaling protein.
TL;DR: A strong correlation is found between phosphorylation-driven activation of the signaling protein NtrC and microsecond time-scale backbone dynamics and a dynamic population shift between two preexisting conformations as the underlying mechanism of activation.
Journal ArticleDOI
Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data.
TL;DR: A novel program has been developed for the interpretation of 15N relaxation rates in terms of macromolecular anisotropic rotational diffusion using the example of the cytochrome c′ from Rhodobacter capsulatus, a four-helix bundle heme protein, for which data at three different field strengths were independently analysed and compared.
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