[NMR paper] Conformational Changes in Ff Phage Protein gVp upon Complexation with Its Viral Single-Stranded DNA Revealed Using Magic-Angle Spinning Solid-State NMR
Conformational Changes in Ff Phage Protein gVp upon Complexation with Its Viral Single-Stranded DNA Revealed Using Magic-Angle Spinning Solid-State NMR
Gene V protein (gVp) of the bacteriophages of the Ff family is a non-specific single-stranded DNA (ssDNA) binding protein. gVp binds to viral DNA during phage replication inside host Escherichia coli cells, thereby blocking further replication and signaling the assembly of new phage particles. gVp is a dimer in solution and in crystal form. A structural model of the complex between gVp and ssDNA was obtained via docking the free gVp to structures of short ssDNA segments and via the detection of...
Is protein deuteration beneficial for proton detected solid-state NMR at and above 100*kHz magic-angle spinning?
Is protein deuteration beneficial for proton detected solid-state NMR at and above 100*kHz magic-angle spinning?
Publication date: Available online 25 July 2017
Source:Solid State Nuclear Magnetic Resonance</br>
Author(s): Diane Cala-De Paepe, Jan Stanek, Kristaps Jaudzems, Kaspars Tars, Loren B. Andreas, Guido Pintacuda</br>
1H-detection in solid-state NMR of proteins has been traditionally combined with deuteration for both resolution and sensitivity reasons, with the optimal level of proton dilution being dependent on MAS rate. Here we present...
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07-26-2017 10:20 AM
[NMR paper] Protein residue linking in a single spectrum for magic-angle spinning NMR assignment.
Protein residue linking in a single spectrum for magic-angle spinning NMR assignment.
Protein residue linking in a single spectrum for magic-angle spinning NMR assignment.
J Biomol NMR. 2015 Jun 16;
Authors: Andreas LB, Stanek J, Le Marchand T, Bertarello A, Paepe DC, Lalli D, Krej?íková M, Doyen C, Öster C, Knott B, Wegner S, Engelke F, Felli IC, Pierattelli R, Dixon NE, Emsley L, Herrmann T, Pintacuda G
Abstract
Here we introduce a new pulse sequence for resonance assignment that halves the number of data sets required...
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06-17-2015 09:27 PM
Protein residue linking in a single spectrum for magic-angle spinning NMR assignment
Protein residue linking in a single spectrum for magic-angle spinning NMR assignment
Abstract
Here we introduce a new pulse sequence for resonance assignment that halves the number of data sets required for sequential linking by directly correlating sequential amide resonances in a single diagonal-free spectrum. The method is demonstrated with both microcrystalline and sedimented deuterated proteins spinning at 60 and 111Â*kHz, and a fully protonated microcrystalline protein spinning at 111Â*kHz, with as little as 0.5Â*mg protein sample. We...
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06-16-2015 04:27 AM
[NMR paper] Solid-state magic-angle spinning NMR of outer-membrane protein G from Escherichia coli.
Solid-state magic-angle spinning NMR of outer-membrane protein G from Escherichia coli.
Related Articles Solid-state magic-angle spinning NMR of outer-membrane protein G from Escherichia coli.
Chembiochem. 2005 Sep;6(9):1679-84
Authors: Hiller M, Krabben L, Vinothkumar KR, Castellani F, van Rossum BJ, Kühlbrandt W, Oschkinat H
Uniformly 13C-,15N-labelled outer-membrane protein G (OmpG) from Escherichia coli was expressed for structural studies by solid-state magic-angle spinning (MAS) NMR. Inclusion bodies of the recombinant, labelled protein...
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12-01-2010 06:56 PM
[NMR paper] Magic-angle spinning solid-state NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis.
Magic-angle spinning solid-state NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis.
Related Articles Magic-angle spinning solid-state NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis.
J Am Chem Soc. 2005 Sep 7;127(35):12291-305
Authors: Franks WT, Zhou DH, Wylie BJ, Money BG, Graesser DT, Frericks HL, Sahota G, Rienstra CM
Magic-angle spinning...
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12-01-2010 06:56 PM
[NMR paper] Magic angle spinning solid-state NMR spectroscopy for structural studies of protein i
Magic angle spinning solid-state NMR spectroscopy for structural studies of protein interfaces. resonance assignments of differentially enriched Escherichia coli thioredoxin reassembled by fragment complementation.
Related Articles Magic angle spinning solid-state NMR spectroscopy for structural studies of protein interfaces. resonance assignments of differentially enriched Escherichia coli thioredoxin reassembled by fragment complementation.
J Am Chem Soc. 2004 Dec 22;126(50):16608-20
Authors: Marulanda D, Tasayco ML, McDermott A, Cataldi M, Arriaran V,...
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11-24-2010 10:03 PM
[NMR paper] Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscop
Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy.
Related Articles Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy.
Nature. 2002 Nov 7;420(6911):98-102
Authors: Castellani F, van Rossum B, Diehl A, Schubert M, Rehbein K, Oschkinat H
The determination of a representative set of protein structures is a chief aim in structural genomics. Solid-state NMR may have a crucial role in structural investigations of those proteins that do not easily form crystals or are not...
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11-24-2010 08:58 PM
Automated protein resonance assignments of magic angle spinning solid-state NMR spect
Automated protein resonance assignments of magic angle spinning solid-state NMR spectra of β1 immunoglobulin binding domain of protein G (GB1)
Abstract Magic-angle spinning solid-state NMR (MAS SSNMR) represents a fast developing experimental technique with great potential to provide structural and dynamics information for proteins not amenable to other methods. However, few automated analysis tools are currently available for MAS SSNMR. We present a methodology for automating protein resonance assignments of MAS SSNMR spectral data and its application to experimental peak lists of the...
Conformational Changes in Ff Phage Protein gVp upon Complexation with Its Viral Single-Stranded DNA Revealed Using Magic-Angle Spinning Solid-State NMR
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