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P K Madhu - One of the best experts on this subject based on the ideXlab platform.

  • selective 1h 1h distance restraints in fully protonated proteins by very fast magic angle spinning solid state nmr
    Journal of Physical Chemistry Letters, 2017
    Co-Authors: Mukul G Jain, Daniela Lalli, Jan Stanek, Chandrakala Gowda, Satya Prakash, Tom S Schwarzer, Tobias Schubeis, Kathrin Castiglione, Loren B Andreas, P K Madhu
    Abstract:

    Very fast magic-angle spinning (MAS > 80 kHz) NMR combined with High-Field Magnets has enabled the acquisition of proton-detected spectra in fully protonated solid samples with sufficient resolution and sensitivity. One of the primary challenges in structure determination of protein is observing long-range 1H–1H contacts. Here we use band-selective spin-lock pulses to obtain selective 1H–1H contacts (e.g., HN–HN) on the order of 5–6 A in fully protonated proteins at 111 kHz MAS. This approach is a major advancement in structural characterization of proteins given that magnetization can be selectively transferred between protons that are 5–6 A apart despite the presence of other protons at shorter distance. The observed contacts are similar to those previously observed only in perdeuterated proteins with selective protonation. Simulations and experiments show the proposed method has performance that is superior to that of the currently used methods. The method is demonstrated on GB1 and a β-barrel membrane...

  • Selective 1H–1H Distance Restraints in Fully Protonated Proteins by Very Fast Magic-Angle Spinning Solid-State NMR
    Journal of Physical Chemistry Letters, 2017
    Co-Authors: Mukul Jain, Daniela Lalli, Chandrakala Gowda, Satya Prakash, Tobias Schubeis, Kathrin Castiglione, Loren B Andreas, Stanek Jan, Tom Schwarzer, P K Madhu
    Abstract:

    Very fast magic-angle spinning (MAS > 80 kHz) NMR combined with High-Field Magnets has enabled the acquisition of proton-detected spectra in fully protonated solid samples with sufficient resolution and sensitivity. One of the primary challenges in structure determination of protein is observing long-range H-1-H-1 contacts. Here we use band-selective spin-lock pulses to obtain selective H-1-H-1 contacts (e.g., H-N-H-N) on the order of 5-6 angstrom in fully protonated proteins at 111 kHz MAS. This approach is a major advancement in structural characterization of proteins given that magnetization can be selectively transferred between protons that are 5-6 angstrom apart despite the presence of other protons at shorter distance. The observed contacts are similar to those previously observed only in perdeuterated proteins with selective protonation. Simulations and experiments show the proposed method has performance that is superior to that of the currently used methods. The method is demonstrated on GB1 and a beta-barrel membrane protein, AlkL.

Stanley J. Opella - One of the best experts on this subject based on the ideXlab platform.

  • Three-dimensional experiment for solid-state NMR of aligned protein samples in High Field Magnets
    Journal of Biomolecular NMR, 2007
    Co-Authors: Alexander A. Nevzorov, Sang Ho Park, Stanley J. Opella
    Abstract:

    A pulse sequence that yields three-dimensional ^1H chemical shift / ^1H-^15N heteronuclear dipolar coupling / ^15N chemical shift solid-state NMR spectra is demonstrated on a uniformly ^15N labeled membrane protein in magnetically aligned phospholipid bilayers. Based on SAMPI4, the pulse sequence yields High resolution in all three dimensions at a ^1H resonance frequency of 900 MHz with the relatively low rf Field strength (33 kHz) available for a lossy aqueous sample with a commercial spectrometer and probe. The ^1H chemical shift frequency dimension is shown to select among amide resonances, which will be useful in studies of larger polytopic membrane proteins where the resonances overlap in two-dimensional spectra. Moreover, the ^1H chemical shift, which can be measured from these spectra, provides an additional orientationally dependent frequency as input for structure calculations.

Daniela Lalli - One of the best experts on this subject based on the ideXlab platform.

  • selective 1h 1h distance restraints in fully protonated proteins by very fast magic angle spinning solid state nmr
    Journal of Physical Chemistry Letters, 2017
    Co-Authors: Mukul G Jain, Daniela Lalli, Jan Stanek, Chandrakala Gowda, Satya Prakash, Tom S Schwarzer, Tobias Schubeis, Kathrin Castiglione, Loren B Andreas, P K Madhu
    Abstract:

    Very fast magic-angle spinning (MAS > 80 kHz) NMR combined with High-Field Magnets has enabled the acquisition of proton-detected spectra in fully protonated solid samples with sufficient resolution and sensitivity. One of the primary challenges in structure determination of protein is observing long-range 1H–1H contacts. Here we use band-selective spin-lock pulses to obtain selective 1H–1H contacts (e.g., HN–HN) on the order of 5–6 A in fully protonated proteins at 111 kHz MAS. This approach is a major advancement in structural characterization of proteins given that magnetization can be selectively transferred between protons that are 5–6 A apart despite the presence of other protons at shorter distance. The observed contacts are similar to those previously observed only in perdeuterated proteins with selective protonation. Simulations and experiments show the proposed method has performance that is superior to that of the currently used methods. The method is demonstrated on GB1 and a β-barrel membrane...

  • Selective 1H–1H Distance Restraints in Fully Protonated Proteins by Very Fast Magic-Angle Spinning Solid-State NMR
    Journal of Physical Chemistry Letters, 2017
    Co-Authors: Mukul Jain, Daniela Lalli, Chandrakala Gowda, Satya Prakash, Tobias Schubeis, Kathrin Castiglione, Loren B Andreas, Stanek Jan, Tom Schwarzer, P K Madhu
    Abstract:

    Very fast magic-angle spinning (MAS > 80 kHz) NMR combined with High-Field Magnets has enabled the acquisition of proton-detected spectra in fully protonated solid samples with sufficient resolution and sensitivity. One of the primary challenges in structure determination of protein is observing long-range H-1-H-1 contacts. Here we use band-selective spin-lock pulses to obtain selective H-1-H-1 contacts (e.g., H-N-H-N) on the order of 5-6 angstrom in fully protonated proteins at 111 kHz MAS. This approach is a major advancement in structural characterization of proteins given that magnetization can be selectively transferred between protons that are 5-6 angstrom apart despite the presence of other protons at shorter distance. The observed contacts are similar to those previously observed only in perdeuterated proteins with selective protonation. Simulations and experiments show the proposed method has performance that is superior to that of the currently used methods. The method is demonstrated on GB1 and a beta-barrel membrane protein, AlkL.

Chandrakala Gowda - One of the best experts on this subject based on the ideXlab platform.

  • selective 1h 1h distance restraints in fully protonated proteins by very fast magic angle spinning solid state nmr
    Journal of Physical Chemistry Letters, 2017
    Co-Authors: Mukul G Jain, Daniela Lalli, Jan Stanek, Chandrakala Gowda, Satya Prakash, Tom S Schwarzer, Tobias Schubeis, Kathrin Castiglione, Loren B Andreas, P K Madhu
    Abstract:

    Very fast magic-angle spinning (MAS > 80 kHz) NMR combined with High-Field Magnets has enabled the acquisition of proton-detected spectra in fully protonated solid samples with sufficient resolution and sensitivity. One of the primary challenges in structure determination of protein is observing long-range 1H–1H contacts. Here we use band-selective spin-lock pulses to obtain selective 1H–1H contacts (e.g., HN–HN) on the order of 5–6 A in fully protonated proteins at 111 kHz MAS. This approach is a major advancement in structural characterization of proteins given that magnetization can be selectively transferred between protons that are 5–6 A apart despite the presence of other protons at shorter distance. The observed contacts are similar to those previously observed only in perdeuterated proteins with selective protonation. Simulations and experiments show the proposed method has performance that is superior to that of the currently used methods. The method is demonstrated on GB1 and a β-barrel membrane...

  • Selective 1H–1H Distance Restraints in Fully Protonated Proteins by Very Fast Magic-Angle Spinning Solid-State NMR
    Journal of Physical Chemistry Letters, 2017
    Co-Authors: Mukul Jain, Daniela Lalli, Chandrakala Gowda, Satya Prakash, Tobias Schubeis, Kathrin Castiglione, Loren B Andreas, Stanek Jan, Tom Schwarzer, P K Madhu
    Abstract:

    Very fast magic-angle spinning (MAS > 80 kHz) NMR combined with High-Field Magnets has enabled the acquisition of proton-detected spectra in fully protonated solid samples with sufficient resolution and sensitivity. One of the primary challenges in structure determination of protein is observing long-range H-1-H-1 contacts. Here we use band-selective spin-lock pulses to obtain selective H-1-H-1 contacts (e.g., H-N-H-N) on the order of 5-6 angstrom in fully protonated proteins at 111 kHz MAS. This approach is a major advancement in structural characterization of proteins given that magnetization can be selectively transferred between protons that are 5-6 angstrom apart despite the presence of other protons at shorter distance. The observed contacts are similar to those previously observed only in perdeuterated proteins with selective protonation. Simulations and experiments show the proposed method has performance that is superior to that of the currently used methods. The method is demonstrated on GB1 and a beta-barrel membrane protein, AlkL.

Satya Prakash - One of the best experts on this subject based on the ideXlab platform.

  • selective 1h 1h distance restraints in fully protonated proteins by very fast magic angle spinning solid state nmr
    Journal of Physical Chemistry Letters, 2017
    Co-Authors: Mukul G Jain, Daniela Lalli, Jan Stanek, Chandrakala Gowda, Satya Prakash, Tom S Schwarzer, Tobias Schubeis, Kathrin Castiglione, Loren B Andreas, P K Madhu
    Abstract:

    Very fast magic-angle spinning (MAS > 80 kHz) NMR combined with High-Field Magnets has enabled the acquisition of proton-detected spectra in fully protonated solid samples with sufficient resolution and sensitivity. One of the primary challenges in structure determination of protein is observing long-range 1H–1H contacts. Here we use band-selective spin-lock pulses to obtain selective 1H–1H contacts (e.g., HN–HN) on the order of 5–6 A in fully protonated proteins at 111 kHz MAS. This approach is a major advancement in structural characterization of proteins given that magnetization can be selectively transferred between protons that are 5–6 A apart despite the presence of other protons at shorter distance. The observed contacts are similar to those previously observed only in perdeuterated proteins with selective protonation. Simulations and experiments show the proposed method has performance that is superior to that of the currently used methods. The method is demonstrated on GB1 and a β-barrel membrane...

  • Selective 1H–1H Distance Restraints in Fully Protonated Proteins by Very Fast Magic-Angle Spinning Solid-State NMR
    Journal of Physical Chemistry Letters, 2017
    Co-Authors: Mukul Jain, Daniela Lalli, Chandrakala Gowda, Satya Prakash, Tobias Schubeis, Kathrin Castiglione, Loren B Andreas, Stanek Jan, Tom Schwarzer, P K Madhu
    Abstract:

    Very fast magic-angle spinning (MAS > 80 kHz) NMR combined with High-Field Magnets has enabled the acquisition of proton-detected spectra in fully protonated solid samples with sufficient resolution and sensitivity. One of the primary challenges in structure determination of protein is observing long-range H-1-H-1 contacts. Here we use band-selective spin-lock pulses to obtain selective H-1-H-1 contacts (e.g., H-N-H-N) on the order of 5-6 angstrom in fully protonated proteins at 111 kHz MAS. This approach is a major advancement in structural characterization of proteins given that magnetization can be selectively transferred between protons that are 5-6 angstrom apart despite the presence of other protons at shorter distance. The observed contacts are similar to those previously observed only in perdeuterated proteins with selective protonation. Simulations and experiments show the proposed method has performance that is superior to that of the currently used methods. The method is demonstrated on GB1 and a beta-barrel membrane protein, AlkL.