Related ArticlesSimultaneous acquisition of 2D and 3D solid-state NMR experiments for sequential assignment of oriented membrane protein samples.
J Biomol NMR. 2015 Mar 7;
Authors: Gopinath T, Mote KR, Veglia G
Abstract
We present a new method called DAISY (Dual Acquisition orIented ssNMR spectroScopY) for the simultaneous acquisition of 2D and 3D oriented solid-state NMR experiments for membrane proteins reconstituted in mechanically or magnetically aligned lipid bilayers. DAISY utilizes dual acquisition of sine and cosine dipolar or chemical shift coherences and long living (15)N longitudinal polarization to obtain two multi-dimensional spectra, simultaneously. In these new experiments, the first acquisition gives the polarization inversion spin exchange at the magic angle (PISEMA) or heteronuclear correlation (HETCOR) spectra, the second acquisition gives PISEMA-mixing or HETCOR-mixing spectra, where the mixing element enables inter-residue correlations through (15)N-(15)N homonuclear polarization transfer. The analysis of the two 2D spectra (first and second acquisitions) enables one to distinguish (15)N-(15)N inter-residue correlations for sequential assignment of membrane proteins. DAISY can be implemented in 3D experiments that include the polarization inversion spin exchange at magic angle via I spin coherence (PISEMAI) sequence, as we show for the simultaneous acquisition of 3D PISEMAI-HETCOR and 3D PISEMAI-HETCOR-mixing experiments.
PMID: 25749871 [PubMed - as supplied by publisher]
Simultaneous acquisition of 2D and 3D solid-state NMR experiments for sequential assignment of oriented membrane protein samples
Simultaneous acquisition of 2D and 3D solid-state NMR experiments for sequential assignment of oriented membrane protein samples
Abstract
We present a new method called DAISY (Dual Acquisition orIented ssNMR spectroScopY) for the simultaneous acquisition of 2D and 3D oriented solid-state NMR experiments for membrane proteins reconstituted in mechanically or magnetically aligned lipid bilayers. DAISY utilizes dual acquisition of sine and cosine dipolar or chemical shift coherences and long living 15N longitudinal polarization to obtain two...
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03-08-2015 01:07 AM
[NMR paper] Sequential protein NMR assignments in the liquid state via sequential data acquisition
Sequential protein NMR assignments in the liquid state via sequential data acquisition
Publication date: Available online 14 December 2013
Source:Journal of Magnetic Resonance</br>
Author(s): Christoph Wiedemann , Peter Bellstedt , Anika Kirschstein , Sabine Häfner , Christian Herbst , Matthias Görlach , Ramadurai Ramachandran</br>
Two different NMR pulse schemes involving sequential 1H data acquisition are presented for achieving protein backbone sequential resonance assignments: (i) acquisition of 3D {HCCNH & HNCACONH} and (ii) collection of 3D {HNCOCANH &...
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12-14-2013 04:48 PM
[NMR paper] Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.
Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.
Related Articles Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.
Nat Protoc. 2013 Nov;8(11):2256-70
Authors: Das N, Murray DT, Cross TA
Abstract
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10-27-2013 12:53 AM
3D DUMAS: Simultaneous acquisition of three-dimensional magic angle spinning solid-state NMR experiments of proteins
3D DUMAS: Simultaneous acquisition of three-dimensional magic angle spinning solid-state NMR experiments of proteins
July 2012
Publication year: 2012
Source:Journal of Magnetic Resonance, Volume 220</br>
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Using the DUMAS (Dual acquisition Magic Angle Spinning) solid-state NMR approach, we created new pulse schemes that enable the simultaneous acquisition of three dimensional (3D) experiments on uniformly 13C, 15N labeled proteins. These new experiments exploit the simultaneous cross-polarization (SIM-CP) from 1H to 13C and 15N to acquire two 3D experiments...
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02-03-2013 10:13 AM
3D DUMAS: Simultaneous Acquisition of Three-Dimensional Magic Angle Spinning Solid-State NMR Experiments of Proteins
3D DUMAS: Simultaneous Acquisition of Three-Dimensional Magic Angle Spinning Solid-State NMR Experiments of Proteins
Publication year: 2012
Source:Journal of Magnetic Resonance</br>
T. Gopinath, Gianluigi Veglia</br>
Using the DUMAS (Dual acquisition Magic Angle Spinning) solid-state NMR approach, we created new pulse schemes that enable the simultaneous acquisition of three dimensional (3D) experiments on uniformly 13C, 15N labeled proteins. These new experiments exploit the simultaneous cross-polarization (SIM-CP) from 1H to 13C and 15N to acquire two 3D experiments...
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04-26-2012 08:10 PM
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers
Abstract Oriented solid-state NMR is the most direct methodology to obtain the orientation of membrane proteins with respect to the lipid bilayer. The method consists of measuring 1H-15N dipolar couplings (DC) and 15N anisotropic chemical shifts (CSA) for membrane proteins that are uniformly aligned with respect to the membrane bilayer. A significant advantage of this approach is that tilt and azimuthal...
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10-10-2011 06:27 AM
Structure Determination in “Shiftless” Solid State NMR of Oriented Protein Samples
Structure Determination in “Shiftless” Solid State NMR of Oriented Protein Samples
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 20 June 2011</br>
Yuanyuan, Yin , Alexander A., Nevzorov</br>
An efficient formalism for calculating protein structures from oriented-sample NMR data in the torsion-angle space is presented. Angular anisotropies of the NMR observables are treated by utilizing an irreducible spherical basis of rotations. An intermediate rotational transformation is introduced that greatly speeds up structural...
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06-21-2011 03:40 PM
[NMR paper] Optimizing oriented planar-supported lipid samples for solid-state protein NMR.
Optimizing oriented planar-supported lipid samples for solid-state protein NMR.
Related Articles Optimizing oriented planar-supported lipid samples for solid-state protein NMR.
Biophys J. 2005 Oct;89(4):2792-805
Authors: Rainey JK, Sykes BD
Sample orientation relative to the static magnetic field of an NMR spectrometer allows study of membrane proteins in the lipid bilayer setting. The straightforward preparation and handling of extremely thin mica substrates with consistent surface properties has prompted us to examine oriented phospholipid...