Tsang, Pearl - University of Cincinnati

个人简介

Pearl Tsang obtained a BA from Barnard College, followed by a PhD at the University of Pennsylvania. After her postdoctoral positions in biological NMR, Dr. Tsang joined the faculty in the Department of Chemistry at UC. Professor Tsang is one of the several biochemists in this Department and as such her general research interests entail elucidation of structure-function relationships of proteins, nucleic acids and biomolecular complexes. One particular class of proteins studied in the Tsang lab corresponds to the aminoacyl tRNA (transfer RNA) synthetaseses. These are enzymes which are crucial for correct covalent linkage of a given amino acid to its corresponding tRNA molecule; this process is also known as 'charging' of the tRNA and is essential for accurate protein translation. These investigations are conducted in order to enhance our understanding of how these proteins carry out their function since their structural and dynamic properties are relevant to their functions. The research conducted in this lab typically involves the production, purification and characterization of the proteins and peptides studied and this involves use of molecular biology and protein purification techniques. The characterization of these molecules involves biophysical and spectroscopic (primarily solution NMR) techniques.

研究领域

Biophysical studies of proteins and nucleic acids; Biomolecular complexes; Biomolecular solution NMR

近期论文

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Yiadom, K.P.A.B., Hammamieh, R., Ukpabi, N., Tsang, P. and Yang, D.C.H. "A Peptide from the extension of Lys-tRNA synthetase binds to transfer RNA and DNA". Peptides (2003), 24, 987-998. Refaei, Mary Anne, Combs, Al, Kojetin, Douglas J, Cavanagh, John, Caperelli, Carol, Rance, Mark, Sapitro, Jennifer, & Tsang, Pearl (2011). Observing selected domains in multi-domain proteins via sortase-mediated ligation and NMR spectroscopy. Journal of biomolecular NMR, 49(1), 3-7. Liu, Sheng, Howell, Michael, Melby, Joel, & Tsang, Pearl (2011). (1)H, (13)C and (15)N resonance assignment of the anticodon binding domain of human lysyl aminoacyl tRNA synthetase. Biomolecular NMR assignments. Liu, Sheng, Decker, Aaron, Howell, Mike, Caperelli, Carol, & Tsang, Pearl (2013). (1)H, (13)C and (15)N resonance assignment of the N-terminal domain of human lysyl aminoacyl tRNA synthetase. Biomolecular NMR assignments, 7(2), 289-92. Ukpabi, N., Sharma, S., Spaller, M.R. and Tsang, P. "1H, 15N and 13C Backbone and Side Chain Assignments of the PDZ3 Domain of PSD-95 Protein". J. Biomolecular NMR (2004), 30, 111. Sankaranarayanan, Jagadis, Bort, Lauren N, Mandel, Sarah M, Chen, Ping, Krause, Jeanette A, Brooks, Elwood E, Tsang, Pearl, & Gudmundsdottir, Anna D (2008). Orbital-Overlap control in the solid-state reactivity of beta-azido-propiophenones: selective formation of cis-azo-dimers. Organic letters, 10(5), 937-40. Manieri, Wanda, Moore, Molly E, Soellner, Matthew B, Tsang, Pearl, & Caperelli, Carol A (2007). Human glycinamide ribonucleotide transformylase: active site mutants as mechanistic probes. Biochemistry, 46(1), 156-63. Ukpabi, Nkoli, Sharma, Sudhir, Spaller, Mark R, & Tsang, Pearl (2004). (1)H, (15)N and (13)C backbone and side chain assignments of PSD-95 PDZ3 protein. Journal of biomolecular NMR, 30(1), 111-2. Yiadom, Kwabena P A B, Hammamieh, Rasha, Ukpabi, Nkoli, Tsang, Pearl, & Yang, David C H (2003). A peptide from the extension of Lys-tRNA synthetase binds to transfer RNA and DNA. Peptides, 24(7), 987-98.