[NMR paper] Membrane topologies of the PGLa antimicrobial peptide and a transmembrane anchor sequence by Dynamic Nuclear Polarization/solid-state NMR spectroscopy.
Membrane topologies of the PGLa antimicrobial peptide and a transmembrane anchor sequence by Dynamic Nuclear Polarization/solid-state NMR spectroscopy.
Related ArticlesMembrane topologies of the PGLa antimicrobial peptide and a transmembrane anchor sequence by Dynamic Nuclear Polarization/solid-state NMR spectroscopy.
Sci Rep. 2016 Feb 15;6:20895
Authors: Salnikov ES, Aisenbrey C, Aussenac F, Ouari O, Sarrouj H, Reiter C, Tordo P, Engelke F, Bechinger B
Abstract
Dynamic Nuclear Polarization (DNP) has been introduced to overcome the sensitivity limitations of nuclear magnetic resonance (NMR) spectroscopy also of supported lipid bilayers. When investigated by solid-state NMR techniques the approach typically involves doping the samples with biradicals and their investigation at cryo-temperatures. Here we investigated the effects of temperature and membrane hydration on the topology of amphipathic and hydrophobic membrane polypeptides. Although the antimicrobial PGLa peptide in dimyristoyl phospholipids is particularly sensitive to topological alterations, the DNP conditions represent well its membrane alignment also found in bacterial lipids at ambient temperature. With a novel membrane-anchored biradical and purpose-built hardware a 17-fold enhancement in NMR signal intensity is obtained by DNP which is one of the best obtained for a truly static matrix-free system. Furthermore, a membrane anchor sequence encompassing 19 hydrophobic amino acid residues was investigated. Although at cryotemperatures the transmembrane domain adjusts it membrane tilt angle by about 10 degrees, the temperature dependence of two-dimensional separated field spectra show that freezing the motions can have beneficial effects for the structural analysis of this sequence.
Cellular solid-state NMR investigation of a membrane protein using dynamic nuclear polarization
From The DNP-NMR Blog:
Cellular solid-state NMR investigation of a membrane protein using dynamic nuclear polarization
Yamamoto, K., et al., Cellular solid-state NMR investigation of a membrane protein using dynamic nuclear polarization. Biochimica et Biophysica Acta (BBA) - Biomembranes, 2015. 1848(1, Part B): p. 342-349.
http://dx.doi.org/10.1016/j.bbamem.2014.07.008
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05-04-2015 04:19 PM
[NMR paper] Cellular Solid-State NMR Investigation of a Membrane Protein Using Dynamic Nuclear Polarization.
Cellular Solid-State NMR Investigation of a Membrane Protein Using Dynamic Nuclear Polarization.
Related Articles Cellular Solid-State NMR Investigation of a Membrane Protein Using Dynamic Nuclear Polarization.
Biochim Biophys Acta. 2014 Jul 10;
Authors: Yamamoto K, Caporini MA, Im SC, Waskell L, Ramamoorthy A
Abstract
While an increasing number of structural biology studies successfully demonstrate the power of high-resolution structures and dynamics of membrane proteins in fully understanding their function, there is...
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07-16-2014 10:46 AM
Cellular Solid-State NMR Investigation of a Membrane Protein Using Dynamic Nuclear Polarization
Cellular Solid-State NMR Investigation of a Membrane Protein Using Dynamic Nuclear Polarization
Publication date: Available online 11 July 2014
Source:Biochimica et Biophysica Acta (BBA) - Biomembranes</br>
Author(s): Kazutoshi Yamamoto , Marc A. Caporini , Sang-Choul Im , Lucy Waskell , Ayyalusamy Ramamoorthy</br>
While an increasing number of structural biology studies successfully demonstrate the power of high-resolution structures and dynamics of membrane proteins in fully understanding their function, there is considerable interest in developing NMR...
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07-12-2014 04:28 AM
Structure and alignment of the membrane-associated antimicrobial peptide arenicin by oriented solid-state NMR spectroscopy.
Structure and alignment of the membrane-associated antimicrobial peptide arenicin by oriented solid-state NMR spectroscopy.
Structure and alignment of the membrane-associated antimicrobial peptide arenicin by oriented solid-state NMR spectroscopy.
Biochemistry. 2011 May 10;50(18):3784-95
Authors: Salnikov ES, Aisenbrey C, Balandin SV, Zhmak MN, Ovchinnikova TV, Bechinger B
The antimicrobial arenicin peptides are cationic amphipathic sequences that strongly interact with membranes. Through a cystine ring closure a cyclic ?-sheet structure is formed...
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07-13-2011 06:42 PM
Structure and Alignment of the Membrane-Associated Antimicrobial Peptide Arenicin by Oriented Solid-State NMR Spectroscopy
Structure and Alignment of the Membrane-Associated Antimicrobial Peptide Arenicin by Oriented Solid-State NMR Spectroscopy
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi1018732/aop/images/medium/bi-2010-018732_0008.gif
Biochemistry
DOI: 10.1021/bi1018732
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/XHW0R5ej4xE
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04-16-2011 02:04 AM
19F NMR analysis of the antimicrobial peptide PGLa bound to native cell membranes fro
19F NMR analysis of the antimicrobial peptide PGLa bound to native cell membranes from bacterial protoplasts and human erythrocytes.
Related Articles 19F NMR analysis of the antimicrobial peptide PGLa bound to native cell membranes from bacterial protoplasts and human erythrocytes.
J Am Chem Soc. 2010 Jul 7;132(26):8822-4
Authors: Ieronimo M, Afonin S, Koch K, Berditsch M, Wadhwani P, Ulrich AS
(19)F NMR is a unique tool to examine the structure of fluorine-labeled peptides in their native cellular environment, due to an exquisite sensitivity...
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10-05-2010 12:11 PM
Probing membrane topology of the antimicrobial peptide distinctin by solid-state NMR
Probing membrane topology of the antimicrobial peptide distinctin by solid-state NMR spectroscopy in zwitterionic and charged lipid bilayers.
Related Articles Probing membrane topology of the antimicrobial peptide distinctin by solid-state NMR spectroscopy in zwitterionic and charged lipid bilayers.
Biochim Biophys Acta. 2010 Aug 15;
Authors: Verardi R, Traaseth NJ, Shi L, Porcelli F, Monfregola L, De Luca S, Amodeo P, Veglia G, Scaloni A
Distinctin is a 47-residue antimicrobial peptide, which interacts with negatively charged membranes and is...
Membrane topologies of the PGLa antimicrobial peptide and a transmembrane anchor sequence by Dynamic Nuclear Polarization/solid-state NMR spectroscopy.
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