Related ArticlesMicromixer-based time-resolved NMR: applications to ubiquitin protein conformation.
Anal Chem. 2003 Feb 15;75(4):956-60
Authors: Kakuta M, Jayawickrama DA, Wolters AM, Manz A, Sweedler JV
Time-resolved NMR spectroscopy is used to studychanges in protein conformation based on the elapsed time after a change in the solvent composition of a protein solution. The use of a micromixer and a continuous-flow method is described where the contents of two capillary flows are mixed rapidly, and then the NMR spectra of the combined flow are recorded at precise time points. The distance after mixing the two fluids and flow rates define the solvent-protein interaction time; this method allows the measurement of NMR spectra at precise mixing time points independent of spectral acquisition time. Integration of a micromixer and a microcoil NMR probe enables low-microliter volumes to be used without losing significant sensitivity in the NMR measurement. Ubiquitin, the model compound, changes its conformation from native to A-state at low pH and in 40% or higher methanol/water solvents. Proton NMR resonances of the His-68 and the Tyr-59 of ubiquitin are used to probe the conformational changes. Mixing ubiquitin and methanol solutions under low pH at microliter per minute flow rates yields both native and A-states. As the flow rate decreases, yielding longer reaction times, the population of the A-state increases. The micromixer-NMR system can probe reaction kinetics on a time scale of seconds.
Rapid identification of protein-protein interfaces for the construction of a complex model based on multiple unassigned signals by using time-sharing NMR measurements.
Rapid identification of protein-protein interfaces for the construction of a complex model based on multiple unassigned signals by using time-sharing NMR measurements.
Rapid identification of protein-protein interfaces for the construction of a complex model based on multiple unassigned signals by using time-sharing NMR measurements.
J Struct Biol. 2011 Apr 9;
Authors: Kodama Y, Reese ML, Shimba N, Ono K, Kanamori E, Dötsch V, Noguchi S, Fukunishi Y, Suzuki EI, Shimada I, Takahashi H
Protein-protein interactions are necessary for various cellular...
NMR-based stable isotope resolved metabolomics in systems biochemistry
NMR-based stable isotope resolved metabolomics in systems biochemistry
Abstract An important goal of metabolomics is to characterize the changes in metabolic networks in cells or various tissues of an organism in response to external perturbations or pathologies. The profiling of metabolites and their steady state concentrations does not directly provide information regarding the architecture and fluxes through metabolic networks. This requires tracer approaches. NMR is especially powerful as it can be used not only to identify and quantify metabolites in an unfractionated mixture such...
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[NMR paper] Effect of pH and copper(II) on the conformation transitions of silk fibroin based on
Effect of pH and copper(II) on the conformation transitions of silk fibroin based on EPR, NMR, and Raman spectroscopy.
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Biochemistry. 2004 Sep 28;43(38):11932-41
Authors: Zong XH, Zhou P, Shao ZZ, Chen SM, Chen X, Hu BW, Deng F, Yao WH
Much attention has been paid to the natural mechanism of silkworm spinning due to the impressive mechanical properties of the natural fibers. Our results in the present work show...
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[NMR paper] Conformational changes in a photosensory LOV domain monitored by time-resolved NMR sp
Conformational changes in a photosensory LOV domain monitored by time-resolved NMR spectroscopy.
Related Articles Conformational changes in a photosensory LOV domain monitored by time-resolved NMR spectroscopy.
J Am Chem Soc. 2004 Mar 24;126(11):3390-1
Authors: Harper SM, Neil LC, Day IJ, Hore PJ, Gardner KH
Phototropins are light-activated kinases from plants that utilize light-oxygen-voltage (LOV) domains as blue light photosensors. Illumination of these domains leads to the formation of a covalent linkage between the protein and an...
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[NMR paper] Leveraging structural approaches: applications of NMR-based screening and X-ray cryst
Leveraging structural approaches: applications of NMR-based screening and X-ray crystallography for inhibitor design.
Related Articles Leveraging structural approaches: applications of NMR-based screening and X-ray crystallography for inhibitor design.
J Synchrotron Radiat. 2004 Jan 1;11(Pt 1):97-100
Authors: Moore J, Abdul-Manan N, Fejzo J, Jacobs M, Lepre C, Peng J, Xie X
In the last several years, NMR strategies in drug discovery have evolved from a primarily structural focus to a set of technologies that are non-structural in nature but...
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[NMR paper] Ubiquitin binding interface mapping on yeast ubiquitin hydrolase by NMR chemical shif
Ubiquitin binding interface mapping on yeast ubiquitin hydrolase by NMR chemical shift perturbation.
Related Articles Ubiquitin binding interface mapping on yeast ubiquitin hydrolase by NMR chemical shift perturbation.
Biochemistry. 1999 Jul 20;38(29):9242-53
Authors: Rajesh S, Sakamoto T, Iwamoto-Sugai M, Shibata T, Kohno T, Ito Y
The interaction between the 26 kDa yeast ubiquitin hydrolase (YUH1), involved in maintaining the monomeric ubiquitin pool in cells, and the 8.5 kDa yeast ubiquitin protein has been studied by heteronuclear...
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[NMR paper] Protein structure refinement based on paramagnetic NMR shifts: applications to wild-t
Protein structure refinement based on paramagnetic NMR shifts: applications to wild-type and mutant forms of cytochrome c.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Protein structure refinement based on paramagnetic NMR shifts: applications to wild-type and mutant forms of cytochrome c.
Protein Sci. 1995 Feb;4(2):296-305
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Micromixer-based time-resolved NMR: applications to ubiquitin protein conformation.
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