Finbloom, J.A., et al., Rotaxane-mediated suppression and activation of cucurbit[6]uril for molecular detection by (129)Xe hyperCEST NMR. Chem Commun (Camb), 2016. 52(15): p. 3119-22.
We report a method for blocking interactions between (129)Xe and cucurbit[6]uril (CB6) until activation by a specific chemical event. We synthesized a CB6-rotaxane that allowed no (129)Xe interaction with the CB6 macrocycle component until a cleavage event released the CB6, which then produced a (129)Xe@CB6 NMR signal. This contrast-upon-activation (129)Xe NMR platform allows for modular synthesis and can be expanded to applications in detection and disease imaging.
Speeding-up exchange-mediated saturation transfer experiments by Fourier transform
Speeding-up exchange-mediated saturation transfer experiments by Fourier transform
Abstract
Protein motions over various time scales are crucial for protein function. NMR relaxation dispersion experiments play a key role in explaining these motions. However, the study of slow conformational changes with lowly populated states remained elusive. The recently developed exchange-mediated saturation transfer experiments allow the detection and characterization of such motions, but require extensive measurement time. Here we show that, by making use of...
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Cucurbit[6]uril is an ultrasensitive (129)Xe NMR contrast agent
From The DNP-NMR Blog:
Cucurbituril is an ultrasensitive (129)Xe NMR contrast agent
Wang, Y. and I.J. Dmochowski, Cucurbituril is an ultrasensitive (129)Xe NMR contrast agent. Chem Commun (Camb), 2015. 51(43): p. 8982-5.
http://www.ncbi.nlm.nih.gov/pubmed/25929681
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06-11-2015 05:15 AM
Hyperpolarized Xenon-Based Molecular Sensors for Label-Free Detection of analytes
From The DNP-NMR Blog:
Hyperpolarized Xenon-Based Molecular Sensors for Label-Free Detection of analytes
Garimella, P.D., et al., Hyperpolarized Xenon-Based Molecular Sensors for Label-Free Detection of analytes. J. Am. Chem. Soc., 2013. 136(1): p. 164-168.
http://pubs.acs.org/doi/abs/10.1021/ja406760r
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02-28-2014 07:08 PM
Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation.
Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation.
Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation.
Biochim Biophys Acta. 2011 Aug 8;
Authors: Mertz B, Struts AV, Feller SE, Brown MF
Abstract
Rhodopsin has served as the primary model for studying G protein-coupled receptors (GPCRs)-the largest group in the human genome, and consequently a primary target for pharmaceutical development. Understanding the functions and activation mechanisms of...
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08-20-2011 03:31 PM
[NMR paper] Sensitivity enhanced NMR spectroscopy by quenching scalar coupling mediated relaxatio
Sensitivity enhanced NMR spectroscopy by quenching scalar coupling mediated relaxation: application to the direct observation of hydrogen bonds in 13C/15N-labeled proteins.
Related Articles Sensitivity enhanced NMR spectroscopy by quenching scalar coupling mediated relaxation: application to the direct observation of hydrogen bonds in 13C/15N-labeled proteins.
J Biomol NMR. 2000 May;17(1):55-61
Authors: Liu A, Hu W, Qamar S, Majumdar A
In this paper, we demonstrate that the sensitivity of triple-resonance NMR experiments can be enhanced...
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11-18-2010 09:15 PM
Cu and Fe metallic ions-mediated oxidation of low-density lipoproteins studied by NMR
Cu and Fe metallic ions-mediated oxidation of low-density lipoproteins studied by NMR, TEM and Z-scan technique.
Related Articles Cu and Fe metallic ions-mediated oxidation of low-density lipoproteins studied by NMR, TEM and Z-scan technique.
Chem Phys Lipids. 2010 Jun;163(6):545-51
Authors: Gómez SL, Monteiro AM, Rabbani SR, Bloise AC, Carneiro SM, Alves S, Gidlund M, Abdalla DS, Neto AM
In this work we report on a study of the morphological changes of LDL induced in vitro by metallic ions (Cu(2+) and Fe(3+)). These modifications were...
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10-22-2010 06:02 AM
[NMR paper] Na(+)-H+ and Na(+)-Li+ exchange are mediated by the same membrane transport protein i
Na(+)-H+ and Na(+)-Li+ exchange are mediated by the same membrane transport protein in human red blood cells: an NMR investigation.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Na(+)-H+ and Na(+)-Li+ exchange are mediated by the same membrane transport protein in human red blood cells: an NMR investigation.
Biochemistry. 1996 Sep 24;35(38):12433-42
Authors: Chi Y, Mo S, Mota de Freitas D
Na(+)-H+ exchange is a transport system present in erythrocytes which plays an important role in...
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08-22-2010 02:20 PM
Detection of unrealistic molecular environments in protein structures based on expect
Abstract Understanding the relationship between protein structure and biological function is a central theme in structural biology. Advances are severely hampered by errors in experimentally determined protein structures. Detection and correction of such errors is therefore of utmost importance. Electron densities in molecular structures obey certain rules which depend on the molecular environment. Here we present and discuss a new approach that relates electron densities computed from a structural model to densities expected from prior observations on identical or closely related molecular...
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Rotaxane-mediated suppression and activation of cucurbit[6]uril for molecular detection by (129)Xe hyperCEST NMR
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