Ultraviolet resonance Raman spectroscopy (UVRR) is a very powerful tool to study molecular structure and dynamics. Resonance Raman scattering requires excitation within an eletronic absorption band and results in a large increase of scattering

it has the additional benefit of avoiding interference from fluorescence. Furthermore

this method make it possible that selectively excite electrons of different functional groups with different excitation wavelengths in order to study the specific parts molecules. Based on the research work the writer did in Pittsburgh University

This paper introduced the status and recent progresses of UVRR spectroscopy used in the study of protein secondary structure and fuctions

the UVRR studies of photochemical isomerization process for aqueous dipeptides NMA and Gly-Gly. The UVRR experimental main points also be demonstrated. A protein consists of one or more amino acides linked by peptide bonds

they are folded into a specific three-dimentional shape maintained by further chemical bonding

such as hydrogen bonds and disulfide bridges. Since the Raman frequencies and intensities of these amide bonds are sensitive to the secondary structure

it is very important to study UV resonance Raman spectroscopy of proteins. Protein spectra obtained using the excitation at 206.5nm are dominated by amide bands.Thirteen proteins give the average pure α-helix

β-sheet and random coil spectra

these average spectra are used as standards to directly determine protein secondary structure. Protein's biological function is determined by its three-dimentional structure. Since the majority of native protein structure self-assemble

these three-dimentional structure must be encode by the protein's primary sequences.Prediction of native protein structure has become more urgent due to the imminent completion of the sequencing of the human genome. The encoding rules must be complex since for most proteins the primary sequence will encode both the native static structure as well as the folding dynamics. These folding dynamics are likely to be complex. A new method has been developed to measure protein folding and unfolding dynamics. Many native proteins unfold(denature) when the solution temperature is raised or lowed. Using the pump-probe technique the folding and unfolding process was monitored in the time scale when they occur. UVRR spectra are obtained at intervals ranging from ten nanoseconds to several hundred nanoseconds following the heat-producing pump pulse.