We have studied the influence of piezoelectric fields on luminescence properties of GaInN strained quantum wells. Our calculation suggests that an electric field of 1.08 MV/cm is induced by the piezoelectric effect in strained Ga0.87In0.13N grown on GaN. The photoluminescence peak energy of the Ga0.87In0.13N strained quantum wells showed blue shift with increasing excitation intensity. Moreover, the well-width dependence of its luminescence peak energy was well explained when the piezoelectric fields were taken into account. These results clearly showed that the piezoelectric field induced the quantum-confined Stark effect.

Aggregation of the amyloid beta-peptide (Abeta) into insoluble fibrils is a key pathological event in Alzheimer's disease. Zn(II) induces the Abeta aggregation at acidic-to-neutral pH, while Cu(II) is an effective inducer only at mildly acidic pH. We have examined Zn(II) and Cu(II) binding modes of Abeta and their pH dependence by Raman spectroscopy. The Raman spectra clearly demonstrate that three histidine residues in the N-terminal hydrophilic region provide primary metal binding sites and the solubility of the metal-Abeta complex is correlated with the metal binding mode. Zn(II) binds to the N(tau) atom of the histidine imidazole ring and the peptide aggregates through intermolecular His(N(tau))-Zn(II)-His(N(tau)) bridges. The N(tau)-metal ligation also occurs in Cu(II)-induced Abeta aggregation at mildly acidic pH. At neutral pH, however, Cu(II) binds to N(pi), the other nitrogen of the histidine imidazole ring, and to deprotonated amide nitrogens of the peptide main chain. The chelation of Cu(II) by histidine and main-chain amide groups results in soluble Cu(II)-Abeta complexes. Under normal physiological conditions, Cu(II) is expected to protect Abeta against Zn(II)-induced aggregation by competing with Zn(II) for histidine residues of Abeta.

Raman spectra of seven tryptophan derivatives in the crystalline state were e x a m i d to find Raman bands whose frequencies reflect the strength of hydrogen bonding at the N,H site of the indole ring or the conformation of the indole ring relative to the amino acid backbone. Two indole ring vibrations, W4 around 1490 em-' and W6 around 1430 cm-', showed a correlation between their Raman frequencies and the infrared frequency of the N-1-H stretching mode, an indicator of hydrogen bond strength. W4 and W6 increase in frequency with increase in hydrogen bond strength and the frequency variation is particularly large for W6. On the other hand, another indole ring vibration, W3, observed around 1550 cm-', changes in frequency as a function of the torsional angle, x2*', of the C-2-C-3-C-t3-C-a linkage. As the absolute value of x2*' becomes larger and the C a atom moves away from the C-2 atom, the W3 frequency increases. In the Raman spectra of proteins excited with visible radiation, the W3 band is usually strong and can be used as a conformational marker, whereas the W4 band is very weak and the W6 band is overlapped by strong scattering due to C-H bending vibrations of aliphatic side-chains. In UV resonance Raman spectra, however, all these Raman bands are enhanced and may provide key information on the hydrogen bonding and conformation of tryptophan side-chains.

The Raman spectrum of a protein contains a wealth of information on the structure and interaction of the protein. To extract the structural information from the Raman spectrum, it is necessary to identify and interpret the marker bands that reflect the structure and interaction in the protein. Recently, new Raman structural markers have been proposed for the tryptophan and histidine side chains by examining the spectra-structure correlations of model compounds. Raman structural markers are now available for the conformation, hydrogen bonding, hydrophobic interaction, and cation-pi interaction of the indole ring of Trp. For His, protonation, tautomerism, and metal coordination of the imidazole ring can be studied by using Raman markers. The high-resolution X-ray crystal structures of proteins provide the basis for testing and modifying the Raman structural markers of Trp and His. The structures derived from Raman spectra are generally consistent with the X-ray crystal structures, giving support for the applicability of most Raman structural makers. Possible modifications and limitations to some marker bands are also discussed.