Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Biophys J. 2010 Nov 17;99(10):3282-9
Authors: Toraya S, Javkhlantugs N, Mishima D, Nishimura K, Ueda K, Naito A
Bombolitin II (BLT2) is one of the hemolytic heptadecapeptides originally isolated from the venom of a bumblebee. Structure and orientation of BLT2 bound to 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) membranes were determined by solid-state (31)P and (13)C NMR spectroscopy. (31)P NMR spectra showed that BLT2-DPPC membranes were disrupted into small particles below the gel-to-liquid crystalline phase transition temperature (T(c)) and fused to form a magnetically oriented vesicle system where the membrane surface is parallel to the magnetic fields above the T(c). (13)C NMR spectra of site-specifically (13)C-labeled BLT2 at the carbonyl carbons were observed and the chemical shift anisotropies were analyzed to determine the dynamic structure of BLT2 bound to the magnetically oriented vesicle system. It was revealed that the membrane-bound BLT2 adopted an ?-helical structure, rotating around the membrane normal with the tilt angle of the helical axis at 33°. Interatomic distances obtained from rotational-echo double-resonance experiments further showed that BLT2 adopted a straight ?-helical structure. Molecular dynamics simulation performed in the BLT2-DPPC membrane system showed that the BLT2 formed a straight ?-helix and that the C-terminus was inserted into the membrane. The ?-helical axis is tilted 30° to the membrane normal, which is almost the same as the value obtained from solid-state NMR. These results suggest that the membrane disruption induced by BLT2 is attributed to insertion of BLT2 into the lipid bilayers.
Dynamic Nuclear Polarization-Enhanced Solid-State NMR of a 13C-Labeled Signal Peptide Bound to Lipid-Reconstituted Sec Translocon
Dynamic Nuclear Polarization-Enhanced Solid-State NMR of a 13C-Labeled Signal Peptide Bound to Lipid-Reconstituted Sec Translocon
Lenica Reggie, Jakob J. Lopez, Ian Collinson, Clemens Glaubitz and Mark Lorch
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja209378h/aop/images/medium/ja-2011-09378h_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja209378h
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Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR.
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR.
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR.
J Am Chem Soc. 2011 Mar 14;
Authors: Yang J, Aslimovska L, Glaubitz C
Environmental factors such as temperature, hydration, and lipid bilayer properties are tightly coupled to the dynamics of membrane proteins. So far, site-resolved data visualizing the protein's response to alterations in these factors are rare, and conclusions had to be drawn from dynamic data averaged over the whole protein...
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03-16-2011 04:15 PM
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR
Jun Yang, Lubica Aslimovska and Clemens Glaubitz
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja109766n/aop/images/medium/ja-2010-09766n_0011.gif
Journal of the American Chemical Society
DOI: 10.1021/ja109766n
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03-15-2011 05:56 AM
The effects of anticalcification treatments and hydration on the molecular dynamics of bovine pericardium collagen as revealed by 13C solid-state NMR.
The effects of anticalcification treatments and hydration on the molecular dynamics of bovine pericardium collagen as revealed by 13C solid-state NMR.
The effects of anticalcification treatments and hydration on the molecular dynamics of bovine pericardium collagen as revealed by 13C solid-state NMR.
Magn Reson Chem. 2010 Sep;48(9):704-11
Authors: deAzevedo ER, Ayrosa AM, Faria GC, Cervantes HJ, Huster D, Bonagamba TJ, Pitombo RN, Rabbani SR
This article describes a solid-state NMR (SSNMR) investigation of the influence of hydration and chemical...
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01-21-2011 12:00 PM
NMR Spectroscopy and Molecular Dynamics Simulation of r(CCGCUGCGG)2 Reveal a Dynamic UU Internal Loop Found in Myotonic Dystrophy Type 1
NMR Spectroscopy and Molecular Dynamics Simulation of r(CCGCUGCGG)2 Reveal a Dynamic UU Internal Loop Found in Myotonic Dystrophy Type 1
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi101896j/aop/images/medium/bi-2010-01896j_0004.gif
Biochemistry
DOI: 10.1021/bi101896j
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01-14-2011 01:59 AM
NMR Spectroscopy and Molecular Dynamics Simulation of r(CCGCUGCGG)2 Reveal a Dynamic UU Internal Loop Found in Myotonic Dystrophy Type 1.
NMR Spectroscopy and Molecular Dynamics Simulation of r(CCGCUGCGG)2 Reveal a Dynamic UU Internal Loop Found in Myotonic Dystrophy Type 1.
NMR Spectroscopy and Molecular Dynamics Simulation of r(CCGCUGCGG)2 Reveal a Dynamic UU Internal Loop Found in Myotonic Dystrophy Type 1.
Biochemistry. 2011 Jan 4;
Authors: Parkesh R, Disney MD, Fountain M
The NMR structure of an RNA with a copy of the 5'CUG/3'GUC motif found in the triplet repeating disorder myotonic dystrophy type 1 (DM1) is disclosed. The lowest energy conformation of the UU pair is a single...
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Linear Mode
