| Summary: | 碩士 === 國立東華大學 === 化學研究所 === 89 === In the field of biochemistry,electrospray ionization mass spectrometry（ESI/MS）is a technique to study the protein conformation and the non-covalent bond interaction between. In our study, we elucidate the pathway of protein folding and unfolding, form the amide hydrogen exchange phenomenon. In the first pant, the cytochrome C was dissolved into different concentration of acetic acid and organic solvent. We facilitate the electrospray ionization mass spectrometry（ESI/MS）technique to acquire the change distribution mass spectra indivinally.At the same time, the ratio of high and low charge is calculated. Form the HX experiments, the protein exchange rate of cytochrome C disserved into different concentration of acetic acid indicates how the protein conform effect the exchange rate. The data shows the higher concentration of acid, the higher the rate constant. The comparison between different species, we can find rates of cytchrome C from bovine is higher the from horse. This indicates the different in structure mar effects the rates. In second part of the research, electrospray ionization mass spectrometry（ESI/MS）is facilitated the study how the metal ion effect the conformation of insulin chain A（ICA）.when ICA bind with change the diversity of ions, the ICA conformation will effect on the HX rates. For 3d transition metal, such as Sc、Cu and Zn,it will increase the exchange rate
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