The secondary structure of proteins in legumes, cereals, milk products and chicken meat was studied by diffuse reflectance infrared spectroscopy in the region of the amide I band. Major secondary structure components ( β-sheets, random coil, α-helix, turns), together with the low- and high-frequency side contributions, were resolved and related to the in vitro digestibility behaviour of the different foods. A strong inverse correlation between the relative spectral weights of the β-sheet structures and in vitro protein digestibility values was measured. Structural modifications in legume proteins induced by autoclaving were monitored by the changes in the amide I spectra. The results indicate that the β-sheet structures of raw legume proteins and the intermolecular β-sheet aggregates, arising upon heating, are primary factors in adversely affecting the digestibility.
Polaronic features similar to those previously observed in the photoinduced
spectra of cuprates have been detected in the reflectivity spectra of
chemically doped parent compounds of high-critical-temperature superconductors,
both $n$-type and $p$-type. In Nd$_2$CuO$_{4-y}$ these features, whose
intensities depend both on doping and temperature, include local vibrational
modes in the far infrared and a broad band centered at $\sim$ 1000 cm$^{-1}$.
The latter band is produced by the overtones of two (or three) local modes and
is well described in terms of a small-polaron model, with a binding energy of
about 500 cm$^{-1}$. Most of the above infrared features are shown to survive
in the metallic phase of Nd$_{2-x}$Ce$_x$Cu0$_{4-y}$, Bi$_2$Sr$_2$CuO$_6$, and
YBa$_2$Cu$_3$O$_{7-y}$, where they appear as extra-Drude peaks. The occurrence
of polarons is attributed to local modes strongly coupled to carriers, as shown
by a comparison with tunneling results.Comment: File latex, 31 p., submitted to Physical Review B. Figures may be
faxed upon reques
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