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1981 (1)
1Author    H. Hauer, H.-D Lüdemann, R. JaenickeRequires cookie*
 Title    Free Activation Energies and Activation Volumes for the Amide Rotation in Some Peptides Studied by High Pressure 'H-High Resolution NMR  
 Abstract    From the pressure dependence o f !H high resolution N M R spectra o f two dipeptides (glycylsarcosine and N-acetyl-L-proline-NH-methylamide in the range 0.1 MPa <.p< . 150 MPa the activation volumes A V* for the am ide rotation are derived. This conform ational transition is characterized for glycylsarcosine by A V* = 4 ± 1 cm3 • m ol-1 and for. the proline derivative by AV* = 1 .5 ± 1 cm3 • m ol-1. From the given results the m axim um contribution o f proline cis ^ trans isomerisation to the pressure dependence o f the rate o f reactivation of proteins can be estimated to ~ — 30% per M Pa and proline present. 
  Reference    Z. Naturforsch. 37c, 51—56 (1982); received Septem ber 221981 
  Published    1982 
  Keywords    Activation Volume, High Pressure, NM R, Peptides, Proline-Isom erization 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0051.pdf 
 Identifier    ZNC-1982-37c-0051 
 Volume    37 
2Author    SeymourSteven Brody, Karel HeremansRequires cookie*
 Title    Pressure Induced Shifts in Spectral Properties of Pigment-Protein Complexes and Photosynthetic Organisms  
 Abstract    Application o f elevated pressure (up to 1200 bars) results in a bathochrom ic shift o f the absorption bands o f photosynthetic pigments. The photosynthetic system s studied include: photosystem I particles, chloroplasts, acetone extracts o f chloroplasts, A U T particles and light harvesting particles o f Rh. sphaeroides, light harvesting particles o f R26. Sim ilar spectral changes are observed in all systems. The spectral shifts appear to be associated w ith pressure-induced changes in the local electric fields o f the pigm ents, rather than changes in the index o f refraction o f the solvent. 
  Reference    Z. Naturforsch. 39c, 1104 (1984); received June 18 1984 
  Published    1984 
  Keywords    Photosynthesis, Chlorophyll, High Pressure, Reaction Centers, C hlorophyll-Protein C om plexes 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-1104.pdf 
 Identifier    ZNC-1984-39c-1104 
 Volume    39 
3Author    Rainer Jaenicke, Hans-Dietrich Liidemann, Gerhard SchmidRequires cookie*
 Title    Pressure, Temperature and pH Dependence of the Absorption Spectrum of Reduced Nicotinamide Adenine Dinucleotide  
 Abstract    Enzymological studies at high hydrostatic pressure generally involve temperature, pH and pressure as variables, owing to the effect of adiabatic compression and the ionization volume o f the buffer system. In the case of N AD dependent oxidoreductases this implies that the extinction coefficient o f the coenzyme may be affected by p, T and pH, apart from the spectral change accompanying the redox reaction. Measurements o f the pressure dependence of the absorbance of N AD H show a slight red shift and a 1% decrease (3% increase) o f the absorbance at 339 nm (360 nm) at 2 kbar. The pH depen­ dence at the given wavelengths amounts to —(2.4 ± 0.1)% per pH unit (25 °C), while the intrinsic temperature effect (after correction for thermal expansion) is o f the order o f -0.2% per degree (2 0 -3 0 °C). Applying buffers with negligible ionization volume, 366 nm is the optimum wavelength for high pressure studies up to 2 kbar because here the pressure dependent spectral changes o f the N ADH absorption vanish. 
  Reference    Z. Naturforsch. 36c, 84—8 (1981); received October 9 1980 
  Published    1981 
  Keywords    Absorption, Dehydrogenases, High Pressure, NADH, Oxidoreductases, pH Dependence, Tem­ perature Dependence 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0084.pdf 
 Identifier    ZNC-1981-36c-0084 
 Volume    36 
4Author    J. Paul, E. V. Goldammer, H. R. WenzelRequires cookie*
 Title    Pressure Induced Structural Fluctuations in Hemoglobin, Studied by EPR-Spectroscopy  
 Abstract    A quartz based cavity for pressure dependent EPR measurements on liquid samples allowing pressures up to 0.6GPa was constructed. First investigations with this setup were done on spin labeled horse hemoglobin derivatives both in ferric and ferrous state of oxidation. The second derivative EPR spectra show changes of the label's mobility, which are not correlated with spin state changes of the Fe-porphyrin complex, but which point out structural fluctuations inside the globin protein matrices. 
  Reference    Z. Naturforsch. 43c, 162—166 (1988); received December 22 1987 
  Published    1988 
  Keywords    High-Pressure, Electron Paramagnetic Resonance, Second Harmonic Detection, Liquid Systems, Hemo-Proteins, Structural Fluctuation, Ligand Binding 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0162.pdf 
 Identifier    ZNC-1988-43c-0162 
 Volume    43