Ceramic cells for high pressure NMR spectroscopy of proteins

Erlach, Markus Beck; Munte, Cláudia Elisabeth; Kremer, Werner; Hartl, Rainer; Rochelt, Dörte; Niesner, Dieter; Kalbitzer, Hans Robert

doi:10.1016/j.jmr.2010.02.011

Cited by 32 publications

(30 citation statements)

References 23 publications

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“…A full-metal autoclave connects the ceramic cell with the closed pressure line (Figure 6). It is similar to the original autoclave provided by Daedalus Innovations [14] but is produced from titanium and contains a safety valve [15] that closes rapidly when the cell brakes.…”

Section: Methodsmentioning

confidence: 99%

“…( a ) The high pressure autoclave holding the ceramic cell is similar to that provided by Daedalus Corporation [14], but has additionally a safety valve analogous to that described earlier by Beck Erlach et al [15]; ( b ) A PET membrane was posed on top of the ceramic cell, and a bored and flattened cylindrical displacement body was inserted into the tube.…”

Section: Methodsmentioning

confidence: 99%

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Pressure Dependence of 15N Chemical Shifts in Model Peptides Ac-Gly-Gly-X-Ala-NH2

et al. 2012

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High pressure NMR spectroscopy has developed into an important tool for studying conformational equilibria of proteins in solution. We have studied the amide proton and nitrogen chemical shifts of the 20 canonical amino acids X in the random-coil model peptide Ac-Gly-Gly-X-Ala-NH2, in a pressure range from 0.1 to 200 MPa, at a proton resonance frequency of 800 MHz. The obtained data allowed the determination of first and second order pressure coefficients with high accuracy at 283 K and pH 6.7. The mean first and second order pressure coefficients and for nitrogen are 2.91 ppm/GPa and −2.32 ppm/GPa2, respectively. The corresponding values and for the amide protons are 0.52 ppm/GPa and −0.41 ppm/GPa2. Residual dependent 1J1H15N-coupling constants are shown.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Pressure Dependence of 15N Chemical Shifts in Model Peptides Ac-Gly-Gly-X-Ala-NH2

et al. 2012

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“…For safety reasons pressure was only applied up to 200 MPa. The autoclave holding the ceramic cell is similar to the original autoclave (Peterson and Wand 2005) provided by Daedalus Innovations LLC but has an integrated safety valve, similar to the security valve described by Beck Erlach et al (2010).…”

Section: High Pressure Systemmentioning

confidence: 99%

Pressure dependence of side chain 13C chemical shifts in model peptides Ac-Gly-Gly-Xxx-Ala-NH2

et al. 2017

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For evaluating the pressure responses of folded as well as intrinsically unfolded proteins detectable by NMR spectroscopy the availability of data from well-defined model systems is indispensable. In this work we report the pressure dependence of C chemical shifts of the side chain atoms in the protected tetrapeptides Ac-Gly-Gly-Xxx-Ala-NH (Xxx, one of the 20 canonical amino acids). Contrary to expectation the chemical shifts of a number of nuclei have a nonlinear dependence on pressure in the range from 0.1 to 200 MPa. The size of the polynomial pressure coefficients B and B is dependent on the type of atom and amino acid studied. For H, N and C the first order pressure coefficient B is also correlated to the chemical shift at atmospheric pressure. The first and second order pressure coefficients of a given type of carbon atom show significant linear correlations suggesting that the NMR observable pressure effects in the different amino acids have at least partly the same physical cause. In line with this observation the magnitude of the second order coefficients of nuclei being direct neighbors in the chemical structure also are weakly correlated. The downfield shifts of the methyl resonances suggest that gauche conformers of the side chains are not preferred with pressure. The valine and leucine methyl groups in the model peptides were assigned using stereospecificallyC enriched amino acids with the pro-R carbons downfield shifted relative to the pro-S carbons.

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“…Finally, we inform about the use of pressure perturbation to modulate enzymatic reactions. The last few years have seen the upsurge in many authoritative reviews and books on various experimental techniques, which will hence not be discussed here . A change of conformation with pressure can be studied with a number of different techniques, including high‐pressure UV/Vis, fluorescence, FTIR and EPR spectroscopy, X‐ray diffraction, as well as scattering experiments such as small‐angle X‐ray scattering (SAXS) and neutron scattering.…”

Section: Introductionmentioning

confidence: 99%

Pressure—A Gateway to Fundamental Insights into Protein Solvation, Dynamics, and Function

2015

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Now that the centennial anniversary of the first report on pressure denaturation of proteins by Nobel Laureate P. W. Bridgman can be celebrated, this Review on the application of high pressure as a key variable for studying the energetics and interactions of proteins appears. We demonstrate that combined temperature-pressure-dependent studies help delineate the free-energy landscape of proteins and elucidate which features are essential in determining their stability. Pressure perturbation also serves as an important tool to explore fluctuations in proteins and reveal their conformational substates. From shaping the free-energy landscape of proteins themselves to that of their interactions, conformational fluctuations not only dictate a plethora of biological processes, but are also implicated in a number of debilitating diseases. Finally, the advantages of using pressure to explore biomolecular assemblies and modulate enzymatic reactions are discussed.

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Ceramic cells for high pressure NMR spectroscopy of proteins

Cited by 32 publications

References 23 publications

Pressure Dependence of 15N Chemical Shifts in Model Peptides Ac-Gly-Gly-X-Ala-NH2

Pressure Dependence of 15N Chemical Shifts in Model Peptides Ac-Gly-Gly-X-Ala-NH2

Pressure dependence of side chain 13C chemical shifts in model peptides Ac-Gly-Gly-Xxx-Ala-NH2

Pressure—A Gateway to Fundamental Insights into Protein Solvation, Dynamics, and Function

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