Sample Optimization and Identification of Signal Patterns of Amino Acid Side Chains in 2D RFDR Spectra of the α-Spectrin SH3 Domain

Pauli, Jutta; Rossum, Barth van; Förster, Hans; Groot, Huub J. M. de; Oschkinat, Hartmut

doi:10.1006/jmre.2000.2029

Cited by 162 publications

(118 citation statements)

References 26 publications

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“…Unlike X-ray crystallography and solid-state NMR total-structure determinations [Straus et al, 1997;Pauli et al, 2000], which require uniform packing and identical atomic coordinates over the entire sample, REDOR NMR does not demand sample homogeneity. The 13 C{ 31 P} REDOR curves in Figure 4, in fact, reflect the existence of distance distributions in the bilayers.…”

Section: Multiple Sterol Populationsmentioning

confidence: 99%

Mapping the locations of estradiol and potent neuroprotective analogues in phospholipid bilayers by REDOR

Cegelski

Rice

O’Connor

et al. 2005

Drug Development Research

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Section: Multiple Sterol Populationsmentioning

confidence: 99%

Mapping the locations of estradiol and potent neuroprotective analogues in phospholipid bilayers by REDOR

Cegelski

Rice

O’Connor

et al. 2005

Drug Development Research

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“…To assign chemical shifts with high precision, the peak line widths should be narrow. Micro-crystallization is a promising method to suppress inhomogeneous line broadening (Pauli et al 2000 ). However, this approach is not applicable, for example, to lipid-bound membrane proteins and protein fibrils.…”

Section: Introductionmentioning

confidence: 99%

Structure determination of uniformly 13C, 15N labeled protein using qualitative distance restraints from MAS solid-state 13C-NMR observed paramagnetic relaxation enhancement

et al. 2016

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Magic angle spinning (MAS) solid-state nuclear magnetic resonance (NMR) is a powerful method for structure determination of insoluble biomolecules. However, structure determination by MAS solid-state NMR remains challenging because it is difficult to obtain a sufficient amount of distance restraints owing to spectral complexity. Collection of distance restraints from paramagnetic relaxation enhancement (PRE) is a promising approach to alleviate this barrier. However, the precision of distance restraints provided by PRE is limited in solid-state NMR because of incomplete averaged interactions and intermolecular PREs. In this report, the backbone structure of the B1 domain of streptococcal protein G (GB1) has been successfully determined by combining the CS-Rosetta protocol and qualitative PRE restraints. The derived structure has a Cα RMSD of 1.49 Å relative to the Xray structure. It is noteworthy that our protocol can determine the correct structure from only three cysteine-EDTA-Mn mutants because this number of PRE sites is insufficient when using a conventional structure calculation method based on restrained molecular dynamics and simulated annealing. This study shows that qualitative PRE restraints can be employed effectively for protein structure determination from a limited conformational sampling space using a protein fragment library. KeywordsSolid-state NMR Magic-angle spinning Protein structure Paramagnetic relaxation enhancement CS-Rosetta Electronic supplementary materialThe online version of this article

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“…[1][2][3][4] The exciting progress in sample-preparation methods, [5] tailored pulse sequences, [4,[6][7][8] and instrumentation now make the investigation of relatively large proteins possible. In spite of these developments, the number of proteins for which an almost complete solid-state assignment is available is still small.…”

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confidence: 99%

Solid‐State NMR of Matrix Metalloproteinase 12: An Approach Complementary to Solution NMR

et al. 2007

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Data transfer. The solid‐state proton‐driven spin diffusion (PDSD) and J‐decoupled PDSD NMR spectra of the microcrystalline catalytic domain of matrix metalloproteinase 12 (MMP‐12, 17 kDa) have been recorded. It is shown that such spectra can be largely assigned in a few days by using the available liquid‐state assignment and validated with an independent sequential assignment based on 3D NCACX and NCOCX PDSD experiments. This demonstrates how quickly the liquid‐state assignment of comparably large protein can be transferred to the solid state.

show abstract

Sample Optimization and Identification of Signal Patterns of Amino Acid Side Chains in 2D RFDR Spectra of the α-Spectrin SH3 Domain

Cited by 162 publications

References 26 publications

Mapping the locations of estradiol and potent neuroprotective analogues in phospholipid bilayers by REDOR

Mapping the locations of estradiol and potent neuroprotective analogues in phospholipid bilayers by REDOR

Structure determination of uniformly 13C, 15N labeled protein using qualitative distance restraints from MAS solid-state 13C-NMR observed paramagnetic relaxation enhancement

Solid‐State NMR of Matrix Metalloproteinase 12: An Approach Complementary to Solution NMR

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