[NMR paper] Revealing Cell-Surface Intramolecular Interactions in the BlaR1 Protein of Methicillin-Resistant Staphylococcus aureus by NMR Spectroscopy.
Revealing Cell-Surface Intramolecular Interactions in the BlaR1 Protein of Methicillin-Resistant Staphylococcus aureus by NMR Spectroscopy.
Related Articles Revealing Cell-Surface Intramolecular Interactions in the BlaR1 Protein of Methicillin-Resistant Staphylococcus aureus by NMR Spectroscopy.
Biochemistry. 2013 Dec 20;
Authors: Frederick TE, Wilson BD, Cha J, Mobashery S, Peng JW
Abstract
In methicillin-resistant Staphylococcus aureus, ?-lactam antibiotic resistance is mediated by the transmembrane protein BlaR1. The antibiotic-sensor...
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12-24-2013 01:04 PM
[NMR paper] Functional dynamics of cell surface membrane proteins
Functional dynamics of cell surface membrane proteins
Publication date: Available online 22 November 2013
Source:Journal of Magnetic Resonance</br>
Author(s): Noritaka Nishida , Masanori Osawa , Koh Takeuchi , Shunsuke Imai , Pavlos Stampoulis , Yutaka Kofuku , Takumi Ueda , Ichio Shimada</br>
Cell surface receptors are integral membrane proteins that receive external stimuli, and transmit signals across plasma membranes. In the conventional view of receptor activation, ligand binding to the extracellular side of the receptor induces conformational changes,...
Revealing Protein Structures in Solid-Phase Peptide Synthesis by 13C Solid-State NMR: Evidence of Excessive Misfolding for Alzheimer’s ?
Revealing Protein Structures in Solid-Phase Peptide Synthesis by 13C Solid-State NMR: Evidence of Excessive Misfolding for Alzheimer’s ?
Songlin Wang and Yoshitaka Ishii
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja212190z/aop/images/medium/ja-2011-12190z_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja212190z
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/6EE7uthrnLg
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01-31-2012 08:34 PM
NMR detection and characterization of sialylated glycoproteins and cell surface polysaccharides
NMR detection and characterization of sialylated glycoproteins and cell surface polysaccharides
Abstract Few solution NMR pulse sequences exist that are explicitly designed to characterize carbohydrates (glycans). This is despite the essential role carbohydrate motifs play in cellâ??cell communication, microbial pathogenesis, autoimmune disease progression and cancer metastasis, and despite that fact that glycans, often shed to extra-cellular fluids, can be diagnostic of disease. Here we present a suite of two dimensional coherence experiments to measure three different correlations...
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09-30-2011 08:01 PM
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Biochemistry. 2011 Sep 26;
Authors: Wang Q, Zhuravleva A, Gierasch LM
Abstract
Biology relies on functional interplay of proteins in the crowded and heterogeneous environment inside cells, and functional protein interactions are often weak and transient. Thus, methods are needed that preserve these...
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09-30-2011 05:59 AM
[NMR paper] Intramolecular dynamics of low molecular weight protein tyrosine phosphatase in monom
Intramolecular dynamics of low molecular weight protein tyrosine phosphatase in monomer-dimer equilibrium studied by NMR: a model for changes in dynamics upon target binding.
Related Articles Intramolecular dynamics of low molecular weight protein tyrosine phosphatase in monomer-dimer equilibrium studied by NMR: a model for changes in dynamics upon target binding.
J Mol Biol. 2002 Sep 6;322(1):137-52
Authors: Akerud T, Thulin E, Van Etten RL, Akke M
Low molecular weight protein tyrosine phosphatase (LMW-PTP) dimerizes in the phosphate-bound...
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11-24-2010 08:58 PM
[NMR paper] NMR solution structure of a cytoplasmic surface loop of the human red cell anion tran
NMR solution structure of a cytoplasmic surface loop of the human red cell anion transporter, band 3.
Related Articles NMR solution structure of a cytoplasmic surface loop of the human red cell anion transporter, band 3.
Biochemistry. 1998 Aug 18;37(33):11670-8
Authors: Askin D, Bloomberg GB, Chambers EJ, Tanner MJ
The membrane domain of the human red cell anion transport protein, band 3, is too large to be studied by solution nuclear magnetic resonance spectroscopy (NMR), and its amphiphilic nature requires the use of detergents for...
Revealing Cell-Surface Intramolecular Interactionsin the BlaR1 Protein of Methicillin-Resistant Staphylococcusaureus by NMR Spectroscopy
Linear Mode
