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15 results on '"Chen, Angela Shuyi"'

4. NMR Analysis of a Novel Enzymatically Active Unlinked Dengue NS2B-NS3 Protease Complex

Author

Kim, Young Mee, primary, Gayen, Shovanlal, additional, Kang, CongBao, additional, Joy, Joma, additional, Huang, Qiwei, additional, Chen, Angela Shuyi, additional, Wee, John Liang Kuan, additional, Ang, Melgious Jin Yan, additional, Lim, Huichang Annie, additional, Hung, Alvin W., additional, Li, Rong, additional, Noble, Christian G., additional, Lee, Le Tian, additional, Yip, Andy, additional, Wang, Qing-Yin, additional, Chia, Cheng San Brian, additional, Hill, Jeffrey, additional, Shi, Pei-Yong, additional, and Keller, Thomas H., additional

Published
2013
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14. NMR structural study of the intracellular loop 3 of the serotonin 5-HT1A receptor and its interaction with calmodulin

Author

Chen, Angela Shuyi, Kim, Young Mee, Gayen, Shovanlal, Huang, Qiwei, Raida, Manfred, and Kang, CongBao

Subjects
*MEMBRANE proteins, *PROTEIN structure, *NUCLEAR magnetic resonance spectroscopy, *SEROTONIN, *CALMODULIN, *G proteins, *CIRCULAR dichroism, *CELL receptors
Abstract

Abstract: The serotonin (5-HT1A) receptor, a G-protein-coupled receptor (GPCR), plays important roles in serotonergic signaling in the central nervous system. The third intracellular loop (ICL3) of the 5-HT1A receptor has been shown to be important for the regulation of this receptor through interactions with proteins such as G-proteins and calmodulin. In this study, the ICL3 of 5-HT1A receptor was expressed in E. coli and purified. Gel filtration and mass spectrometry were used to confirm the molecular weight of the purified ICL3. Secondary structure analysis using circular dichroism (CD) demonstrated the presence of α-helical structures. Backbone assignment of ICL3 was achieved using three-dimensional experiments. A chemical shift index and Talos+ analysis showed that residues E326 to R339 form α-helical structure. Residues G256 to S269 of ICL3 were shown to be a novel region that has a molecular interaction with calmodulin in titration assays. Peptide derived from the ICL3 containing residues from G256 to S269 also showed molecular interaction with calmodulin. [Copyright &y& Elsevier]

Published
2011
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15. ¹H, ¹³C and ¹⁵N chemical shift assignments for an intracellular proteinase inhibitor of Bacillus subtilis.

Author

Li Q, Chen AS, Gayen S, and Kang C

Subjects
Amino Acid Sequence, Carbon Isotopes, Molecular Sequence Data, Nitrogen Isotopes, Protein Structure, Secondary, Bacillus subtilis metabolism, Bacterial Proteins chemistry, Intracellular Space metabolism, Nuclear Magnetic Resonance, Biomolecular, Protease Inhibitors chemistry, Protons
Abstract

Intracellular proteinases (ISPs) are the main component of the bacilli degradome and a distinctive class in different bacilli. An intracellular proteinase inhibitor of the bacteria Bacillus subtillis was shown to regulate the activity of ISP-1. To study the structure of this inhibitor, we report the resonance assignment for this protein with 119 amino acid. The data will allow us to perform structural study on this inhibitor to understand its mechanism for ISP-1 inhibition.

Published
2013
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