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Biomedical subjects

L Genzel

Publications and source records attributed to L Genzel.

11 recordsLinked to original sources
PubMed1993

Far-infrared study of the vibrational modes of 5'-GMP gels and crystals of Na+ and K+.

Five Far-Infrared (50-600 cm-1) spectra are presented: the sodium and potassium salts of 5' Guanosine Monophosphate (GMP), each salt in both the gel and crystal conformations, and poly(rG). Measurements were performed at a sample temperature of 10 K under vacuum with a liquid He-cooled bolometer. The spectra were fit with Lorentzians and assignments are suggested. There are noteworthy differences in oscillator strengths and frequencies of the bands between all spectra. We report the tentative observation of a 100 cm-1 mode which is in the neighborhood of a mode observed by Raman spectroscopy in solution (1) and dried gels (2).

Crystallization↗
PubMed1984

Picosecond relaxations in hydrated lysozyme observed by mm-wave spectroscopy.

Dielectric absorption measurements at mm-wave frequencies (50 GHz. . . 150 GHz) are reported for lysozyme at different hydration levels. The measurements were extended over the temperature range from liquid helium to room temperature using the untuned cavity technique. For dried lysozyme (water content less than or equal to 0.5%, w/w) a nearly linear increase with frequency and an exponential increase with temperature of the absorption coefficient is observed between 50 K and 300 K. This frequency and temperature dependence is described by relaxation processes in asymmetric double-well potentials with relaxation times in the picosecond range. Hydration yields a nearly frequency-independent contribution to the absorption, which arises only at temperatures above 120 K. The frequency independence indicates relaxation rates for the bound water that are small compared to mm-wave frequencies. Thereby the contribution of bound water can clearly be distinguished from the fast intrinsic processes. An assignment of these picosecond relaxations to the NH . . . OC hydrogen bond of the peptide backbone is suggested.

Muramidase↗
PubMedDate not supplied

Search for millimeter microwave effects on enzyme or protein functions.

Recent observations of nonthermal, resonant biological responses to weak millimeter microwave irradiation have led us to investigate whether similar influences exist on enzymatic functions in vitro. We chose (i) the reduction of ethanol in the presence of alcohol dehydrogenase and (ii) the cooperative binding of oxygen on hemoglobin. Using an irradiation intensity near 10 mW/cm2 the frequency was continuously varied from 40 to 115 GHz with a resolution of a few MHz. No microwave influences were detectable within our experimental sensitivity of about 0.1% of the reaction rate in (i), or of the amount of bound oxygen at half saturation in (ii).

Alcohol Oxidoreductases↗