[NMR paper] Multidimensional Solid-State NMR of a Functional Multiprotein Chemoreceptor Array.
Multidimensional Solid-State NMR of a Functional Multiprotein Chemoreceptor Array.
Related Articles Multidimensional Solid-State NMR of a Functional Multiprotein Chemoreceptor Array.
Biochemistry. 2016 Jun 13;
Authors: Harris MJ, Struppe JO, Wylie BJ, McDermott AE, Thompson LK
Abstract
The bacterial chemoreceptor complex governs signal detection and the upstream elements of chemotactic behavior, but the detailed molecular mechanism is still unclear. We have assembled native-like functional arrays of an aspartate receptor...
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[NMR paper] Nano-Mole Scale Side-Chain Signal Assignment by 1H-Detected Protein Solid-State NMR by Ultra-Fast Magic-Angle Spinning and Stereo-Array Isotope Labeling.
Nano-Mole Scale Side-Chain Signal Assignment by 1H-Detected Protein Solid-State NMR by Ultra-Fast Magic-Angle Spinning and Stereo-Array Isotope Labeling.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png Related Articles Nano-Mole Scale Side-Chain Signal Assignment by 1H-Detected Protein Solid-State NMR by Ultra-Fast Magic-Angle Spinning and Stereo-Array Isotope Labeling.
PLoS One. 2015;10(4):e0122714
Authors: Wang S, Parthasarathy S, Nishiyama Y, Endo Y, Nemoto T, Yamauchi K, Asakura T,...
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04-11-2015 12:04 AM
[NMR paper] Nanotube Array Method for Studying Lipid-Induced Conformational Changes of a Membrane Protein by Solid-State NMR.
Nanotube Array Method for Studying Lipid-Induced Conformational Changes of a Membrane Protein by Solid-State NMR.
Nanotube Array Method for Studying Lipid-Induced Conformational Changes of a Membrane Protein by Solid-State NMR.
Biophys J. 2015 Jan 6;108(1):5-9
Authors: Marek A, Tang W, Milikisiyants S, Nevzorov AA, Smirnov AI
Abstract
Anodic aluminum oxide substrates with macroscopically aligned homogeneous nanopores of 80*nm in diameter enable two-dimensional, solid-state nuclear magnetic resonance studies of lipid-induced...
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01-08-2015 01:29 PM
Nanotube Array Method for Studying Lipid-Induced Conformational Changes of a Membrane Protein by Solid-State NMR
Nanotube Array Method for Studying Lipid-Induced Conformational Changes of a Membrane Protein by Solid-State NMR
Publication date: 6 January 2015
Source:Biophysical Journal, Volume 108, Issue 1</br>
Author(s): Antonin Marek , Wenxing Tang , Sergey Milikisiyants , Alexander*A. Nevzorov , Alex*I. Smirnov</br>
Anodic aluminum oxide substrates with macroscopically aligned homogeneous nanopores of 80*nm in diameter enable two-dimensional, solid-state nuclear magnetic resonance studies of lipid-induced conformational changes of uniformly 15N-labeled Pf1 coat protein...
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01-07-2015 11:26 AM
Heat management strategies for solid-state NMR of functional proteins
Heat management strategies for solid-state NMR of functional proteins
September 2012
Publication year: 2012
Source:Journal of Magnetic Resonance, Volume 222</br>
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Modern solid-state NMR methods can acquire high-resolution protein spectra for structure determination. However, these methods use rapid sample spinning and intense decoupling fields that can heat and denature the protein being studied. Here we present a strategy to avoid destroying valuable samples. We advocate first creating a sacrificial sample, which contains unlabeled protein (or no protein) in buffer...
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02-03-2013 10:13 AM
Heat Management Strategies for Solid-state NMR of Functional Proteins
Heat Management Strategies for Solid-state NMR of Functional Proteins
Publication year: 2012
Source:Journal of Magnetic Resonance</br>
Daniel J. Fowler, Michael J. Harris, Lynmarie K. Thompson</br>
Modern solid-state NMR methods can acquire high-resolution protein spectra for structure determination. However, these methods use rapid sample spinning and intense decoupling fields that can heat and denature the protein being studied. Here we present a strategy to avoid destroying valuable samples. We advocate first creating a sacrificial sample, which contains unlabeled...
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07-14-2012 01:53 PM
[NMR paper] Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins u
Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins using spin-state selection.
Related Articles Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins using spin-state selection.
J Am Chem Soc. 2003 Oct 1;125(39):11816-7
Authors: Duma L, Hediger S, Brutscher B, Böckmann A, Emsley L
We show that the resolution of homonuclear multidimensional solid-state NMR correlation experiments can be significantly improved using transition selection and spin-state-selective polarization transfer...
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11-24-2010 09:16 PM
[NMR paper] Prospects for resonance assignments in multidimensional solid-state NMR spectra of un
Prospects for resonance assignments in multidimensional solid-state NMR spectra of uniformly labeled proteins.
Related Articles Prospects for resonance assignments in multidimensional solid-state NMR spectra of uniformly labeled proteins.
J Biomol NMR. 1996 Oct;8(3):239-51
Authors: Tycko R
The feasibility of assigning the backbone 15N and 13C NMR chemical shifts in multidimensional magic angle spinning NMR spectra of uniformly isotopically labeled proteins and peptides in unoriented solid samples is assessed by means of numerical simulations....
Multidimensional Solid-State Nuclear Magnetic Resonanceof a Functional Multiprotein Chemoreceptor Array
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