Related ArticlesProbing a cell-embedded megadalton protein complex by DNP-supported solid-state NMR.
Nat Methods. 2015 May 18;
Authors: Kaplan M, Cukkemane A, van Zundert GC, Narasimhan S, Daniëls M, Mance D, Waksman G, Bonvin AM, Fronzes R, Folkers GE, Baldus M
Abstract
Studying biomolecules at atomic resolution in their native environment is the ultimate aim of structural biology. We investigated the bacterial type IV secretion system core complex (T4SScc) by cellular dynamic nuclear polarization-based solid-state nuclear magnetic resonance spectroscopy to validate a structural model previously generated by combining in vitro and in silico data. Our results indicate that T4SScc is well folded in the cellular setting, revealing protein regions that had been elusive when studied in vitro.
PMID: 25984698 [PubMed - as supplied by publisher]
[NMR paper] Ligand orientation in a membrane-embedded receptor site revealed by solid-state NMR with paramagnetic relaxation enhancement.
Ligand orientation in a membrane-embedded receptor site revealed by solid-state NMR with paramagnetic relaxation enhancement.
Related Articles Ligand orientation in a membrane-embedded receptor site revealed by solid-state NMR with paramagnetic relaxation enhancement.
Org Biomol Chem. 2015 Jan 13;
Authors: Whittaker CA, Patching SG, Esmann M, Middleton DA
Abstract
NMR relaxation enhancement by paramagnetic metals provides powerful restraints on the three-dimensional structures of proteins in solution, and this approach has...
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01-15-2015 06:10 PM
[NMR paper] Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach.
Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach.
Related Articles Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach.
J Biomol NMR. 2015 Jan 8;
Authors: Sinnige T, Houben K, Pritisanac I, Renault M, Boelens R, Baldus M
Abstract
The ?-barrel assembly machinery (BAM) is involved in folding and insertion of outer membrane proteins in Gram-negative bacteria, a process that is still poorly...
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01-09-2015 03:58 PM
Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach
Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach
Abstract
The β-barrel assembly machinery (BAM) is involved in folding and insertion of outer membrane proteins in Gram-negative bacteria, a process that is still poorly understood. With its 790 residues, BamA presents a challenge to current NMR methods. We utilized a â??divide and conquerâ?? approach in which we first obtained resonance assignments for BamAâ??s periplasmic POTRA domains 4 and 5 by solution NMR. Comparison of...
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01-08-2015 01:02 AM
[NMR paper] Probing membrane protein structure using water polarization transfer solid-state NMR.
Probing membrane protein structure using water polarization transfer solid-state NMR.
Related Articles Probing membrane protein structure using water polarization transfer solid-state NMR.
J Magn Reson. 2014 Aug 25;
Authors: Williams JK, Hong M
Abstract
Water plays an essential role in the structure and function of proteins, lipid membranes and other biological macromolecules. Solid-state NMR heteronuclear-detected (1)H polarization transfer from water to biomolecules is a versatile approach for studying water-protein,...
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09-18-2014 01:33 PM
[NMR paper] Probing Membrane Protein Structure Using Water Polarization Transfer Solid-State NMR
Probing Membrane Protein Structure Using Water Polarization Transfer Solid-State NMR
Publication date: Available online 25 August 2014
Source:Journal of Magnetic Resonance</br>
Author(s): Jonathan K. Williams , Mei Hong</br>
Water plays an essential role in the structure and function of proteins, lipid membranes and other biological macromolecules. Solid-state NMR heteronuclear-detected 1H polarization transfer from water to biomolecules is a versatile approach for studying water-protein, water-membrane, and water-carbohydrate interactions in biology. We review...
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08-26-2014 01:14 AM
[NMR paper] Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein.
Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein.
Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein.
Nat Methods. 2013 Sep 8;
Authors: Wang S, Munro RA, Shi L, Kawamura I, Okitsu T, Wada A, Kim SY, Jung KH, Brown LS, Ladizhansky V
Abstract
Determination of structure of integral membrane proteins, especially in their native environment, is a formidable challenge in structural biology. Here we demonstrate that magic angle spinning...
[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...
Probing a cell-embedded megadalton protein complex by DNP-supported solid-state NMR.
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