Proteins are the machines of life. Protein functions, in turn are determined by their three dimensional structure. Alterations in the shape of a single protein can often determine the health or diseased state of an individual. Our lab is focused on determining the structure-functional relationship of proteins of pathological interests. We further explore the possibility of developing drugs to combat diseases caused by mutations in these proteins. We apply state-of-the-arts NMR and other physic-chemical and molecular biology techniques to these aims. Currently our laboratory works on the following protein systems:

• SUMO-mediated signal transduction:
  Post-translational modification by Small Ubiquitin-like MOdifier (SUMO) proteins regulates a diverse array of cellular events.

  We investigated:
  1. The structural and functional roles of Daxx-SIM (SUMO Interaction Motif) interaction;
  2. The effect of phosphorylation and acetylation in SUMO paralogue-selective binding and apoptosis modulation ;
  3. The molecular basis of poly-SIM/poly-SUMO recognition in RNF4;
  4. The mechanism of promyelocytic leukemia protein sumoylation.

• The ferrous iron transport system, Feo, from K. pneumoniae:
  K. pneumoniae is an emerging strain of gram-negative bacillus that causes community-acquired primary liver abscess with sepsis and bacteria in Taiwan. We are investigating molecular mechanism of K. pneumoniae ferrous iron transport system, Feo, which consists of three proteins (FeoA, FeoB and FeoC).

SARS-CoV RNP

• Packaging of SARS coronavirus nucelocapsid protein:
  SARS-CoV is the itiological agent of severe acute respiratory syndrome (SARS). The virion consists of a nucelocapsid core surrounded by an envelope containing three membrane proteins, spike (S), membrane (M) and envelope (E). The RNA is packaged by the nucelocapsid protein (N) into a helical nucelocapsid. SARS-CoV N is a major target in the development of early diagnosis kits for SARS and a potential target for therapeutic agents.

• Proteinopathy of TDP-43:
  TDP-43 is a DNA/RNA-binding protein associated with different neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS), frontotemporal lobar degeneration (FTLD-U). Alzheimer's disease, Parkinson's disease and Huntington's disease. Thus, it is of great interest to investigate the molecular basis of the TDP-43 associated proteinopathies.

• The group 5 major allergen of Bromia tropicalis, Blo t 5 (Allergen):
  Allergen derived from Bromia tropicalis has been estimated to casue one billion cases of allergy world wide and Blo t 5 is the major allergen of Bromia tropicalis

• We are also in charge of High-field NMR Center (HFNMRC) for supporting biomolecular NMR research in Taiwan. The HFNMRC is equipped with several high-field NMR spectrometers at 500, 600, 800 and 850 MHz.