As a common defense mechanism in Hymenoptera, bee venom has complex components. Systematic and comprehensive analysis of bee venom components can aid in early evaluation, accurate diagnosis, and protection of organ function in humans in cases of bee stings. To determine the differences in bee venom composition and metabolic pathways between Apis cerana and Apis mellifera, proton nuclear magnetic resonance (¹ H-NMR) technology was used to detect the metabolites in venom samples. A total of 74...
[NMR paper] Using Abundant 1H Polarization to Enhance the Sensitivity of Solid-State NMR Spectroscopy
Using Abundant 1H Polarization to Enhance the Sensitivity of Solid-State NMR Spectroscopy
Solid-state NMR spectroscopy has been playing a significant role in elucidating the structures and dynamics of materials and proteins at the atomic level for decades. As an extremely abundant nucleus with a very high gyromagnetic ratio, protons are widely present in most organic/inorganic materials. Thus, this Perspective highlights the advantages of proton detection at fast magic-angle spinning (MAS) and presents strategies to utilize and exhaust ¹H polarization to achieve signal sensitivity...
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[NMR paper] Differentially Isotope-Labeled Nucleosomes to Study Asymmetric Histone Modification Crosstalk by Time-Resolved NMR Spectroscopy.
Differentially Isotope-Labeled Nucleosomes to Study Asymmetric Histone Modification Crosstalk by Time-Resolved NMR Spectroscopy.
Related Articles Differentially Isotope-Labeled Nucleosomes to Study Asymmetric Histone Modification Crosstalk by Time-Resolved NMR Spectroscopy.
Angew Chem Int Ed Engl. 2016 May 24;
Authors: Liokatis S, Klingberg R, Tan S, Schwarzer D
Abstract
Post-translational modifications (PTMs) of histones regulate chromatin structure and function. Because nucleosomes contain two copies each of the four core...
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[NMR paper] Systematic identification of protein-metabolite interactions in complex metabolite mixtures by ligand-detected NMR spectroscopy.
Systematic identification of protein-metabolite interactions in complex metabolite mixtures by ligand-detected NMR spectroscopy.
Systematic identification of protein-metabolite interactions in complex metabolite mixtures by ligand-detected NMR spectroscopy.
Biochemistry. 2016 Apr 11;
Authors: Nikolaev YV, Kochanowski K, Link H, Sauer U, Allain FH
Abstract
Protein-metabolite interactions play a vital role in the regulation of numerous cellular processes. Consequently, identifying such interactions is a key prerequisite for...
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[NMR paper] Natural abundant (17) O NMR in a 1.5-T Halbach magnet.
Natural abundant (17) O NMR in a 1.5-T Halbach magnet.
Natural abundant (17) O NMR in a 1.5-T Halbach magnet.
Magn Reson Chem. 2015 Jan 16;
Authors: Sørensen MK, Bakharev ON, Jensen O, Nielsen NC
Abstract
We present mobile, low-field (17) O NMR as a means for monitoring oxygen in liquids. Whereas oxygen is one of the most important elements, oxygen NMR is limited by a poor sensitivity related to low natural abundance and gyro-magnetic ratio of the NMR active (17) O isotope. Here, we demonstrate (17) O NMR detection at a...
Exploring the Backbone Dynamics of Native Spider Silk Proteins in Black Widow Silk Glands with Solution-state NMR Spectroscopy
Exploring the Backbone Dynamics of Native Spider Silk Proteins in Black Widow Silk Glands with Solution-state NMR Spectroscopy
Publication date: Available online 13 June 2014
Source:Polymer</br>
Author(s): Dian Xu , Jeffery L. Yarger , Gregory P. Holland</br>
Spider dragline silk is an outstanding biopolymer with a strength that exceeds steel by weight and a toughness greater than high-performance fibers like Kevlar. For this reason, understanding how a spider converts the gel-like, aqueous protein spinning dope within the major ampullate (MA) gland into a super...
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[NMR paper] NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1
NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors.
Related Articles NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors.
Protein Sci. 2000 May;9(5):976-84
Authors: Cierpicki T, Bania J, Otlewski J
The three-dimensional structure of the 56 residue polypeptide Apis mellifera chymotrypsin/cathepsin G inhibitor 1 (AMCI-1) isolated from honey bee hemolymph was...
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[NMR paper] A structural homologue of colipase in black mamba venom revealed by NMR floating disu
A structural homologue of colipase in black mamba venom revealed by NMR floating disulphide bridge analysis.
Related Articles A structural homologue of colipase in black mamba venom revealed by NMR floating disulphide bridge analysis.
J Mol Biol. 1998;283(1):205-19
Authors: Boisbouvier J, Albrand JP, Blackledge M, Jaquinod M, Schweitz H, Lazdunski M, Marion D
The solution structure of mamba intestinal toxin 1 (MIT1), isolated from Dendroaspis polylepis polylepis venom, has been determined. This molecule is a cysteine-rich polypeptide...
(1) H-NMR revealed pyruvate as a differentially abundant metabolite in the venom glands of Apis cerana and Apis mellifera
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