| Summary: | 碩士 === 國立陽明大學 === 醫學生物技術暨檢驗學系 === 104 === In nature, the protein modifications of archaea was closer to eukaryote than that of bacteria, and the genome of archaea is easier to manipulate than eukaryote. Therefore, archaea has potential commercial value. Post-translational modification of proteins (PTMs) play an important role in protein structure, function, and hemostasis.
Experimentally, I isolated the ribosomal proteins of a halophilic archaea, Halobaterium sp. NRC-1. Second, I applied liquid chromatography tandem mass spectrometry (LC-MS/MS) to analyze the ribosomal proteins. Further, I compared the difference of peptide sequences identified by tradition fragmentation, and other partial fragmentation methods. Third, according to the mapping of spectra to recognize the post-translational modifications, including methylation and acetylation in the detected peptides. Finally, I revealed several ribosomal PTMs.
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