Positions

Professor
Biochemistry-Ma Lab
Baylor College of Medicine
Houston, TX, US
Lodwick T. Bolin Professor in Biochemistry
Biochemistry
Baylor College of Medicine and Rice University
Houston, Texas, United States
Member
Dan L Duncan Comprehensive Cancer Center
Baylor College of Medicine
Houston, Texas, United States

Education

Advanced Training from Harvard University
Ph.D. from Boston University
B.S. from Fu-Dan University

Honors & Awards

Elected Fellow of the American Institute for Medical Biological Engineering
2008 Michael E. DeBakey Excellence in Research Award
Elected Fellow of the American Association for the Advancement of Science (AAAS)
Elected Fellow of the American Physical Society (APS)
2004 Norman Hackerman Award for Chemical Research
The award is for recognizing his outstanding contributions to biochemistry, biophysics and structural biology. It consists of a $100,000 check, a certificate and a crystal sculpture symbolizing a rising star.
Faculty Early Career Development (CAREER) Award
Award for Distinguished Young Scholars Abroad
Burroughs Wellcome Fund PMMB Postdoctoral Fellow
Advanced Study Institutes Travel Award
The Finn Wold Travel Award
Postdoctoral Fellow of the National Institutes of Health (NIH)
Super-computing Grant
Free Subscription of J. Phys. Chem. for Cray Super-computing Award

Professional Interests

  • Viral Pathogens
  • Human
  • Bioinformatics
  • Nano Medicine and Drug Design
  • Biophysics and Computational Biology
  • Protein Structure-Function and Protein Folding
  • Structural Biology and Macromolecular Assemblies
  • Signal Transduction
  • Stem Cell Biology and Cell Fate Determination
  • Gene Expression and Regulation
  • Chromosomes, Chromatin, and DNA Biology
  • Cancer
  • Development and Evoluation
  • Genomics, Proteomics, and Metabolomics
  • Molecular Basis of Human Disease and Behavior

Professional Statement

Multi-resolution and Multi-length Scale Simulation of Supermolecular Complexes

Large-scale conformational transitions in protein structures play an important role in a variety of cellular processes. Understanding such transitions is one of the central tasks of modern biophysics and structural biology. Among all the available structural and biophysical methods, computer simulation is a powerful method that allows one to model the motions of proteins in atomic details. The research projects primarily focus on systems that involve coordinated large domain movements. Our recent work on the molecular chaperonin GroEL and F1-ATPase provided paradigms for this type of research, and it also demonstrates that molecular dynamics simulation has come into an age of realistically modeling very large protein complexes.

Structural Refinement for X-ray, cryo-EM and Fiber Diffraction

In recent history, molecular dynamics simulation has been successfully employed to significantly improve the structure refinement in X-ray crystallography. However, as structural biology moves towards meeting the new challenges imposed by the study of more complex and more dynamic biological systems, more advanced computational methods are urgently needed to effectively deal with molecular motions in structure refinement. Our group is committed to improving structure refinement in X-ray crystallography, electron cryomicroscopy (cryo-EM) and fiber diffraction. Quantized elastic deformational model (QEDM) has been demonstrated highly effective in assisting cryo-EM single-particle reconstruction of intrinsically flexible biological systems. Substructure synthesis method (SSM) is extremely powerful for enhancing the structure refinement against fiber diffraction data. Moreover, important progress of improving X-ray structure refinement has been recently achieved. These lines of research will undoubtedly provide powerful tools for structure refinement in the wider fields of structural biology.

Structure Modeling and Prediction

With the advance of cryo-EM single-particle reconstruction, more and more intermediate-resolution structures are available. It would be extremely useful if protein secondary structures and protein topology can be determined from intermediate-resolution data. Our group has recently developed sheetminer and sheettracer that are capable of accurately locating beta-sheets and building beta-strands in intermediate-resolution density maps. Once protein secondary structures are in place, protein topology can be determined using approaches recently developed in our group. These methods will greatly enhance one's ability to obtain meaningful information about protein structure and function from intermediate-resolution data.

Selected Publications

Memberships

American Physical Society
American Crystallographic Association
Biomedical Engineering Society
Biophysical Society
American Chemical Society
Protein Society