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  • +886-2-2789-9043 (Lab) (Room No: N117)
  • +886-2-2652-3031 (Office)
  • +886-2-2788-7641 (Fax)

  • Computational Biophysics
  • Computational Chemistry
  • Bioinformatics

Education and Positions:
  • 1984, Ph.D. in Chemical Physics, University of Minnesota, Minneapolis

    1979, B.S. in Chemistry, Royal Holloway College, London University


Highlight Detail

Differential Role of the Protein Matrix on the Binding of a Catalytic Aspartate to Mg2+ vs Ca2+: Application to Ribonuclease H.

Dr. Lim, Carmay
J Am Chem Soc., Apr 23, 2013

Divalent metal cations are essential cofactors for many enzyme functions. Although Mg2+ is the native cofactor in many enzymes such as ribonuclease H, its competitor Ca2+ may also bind to the enzyme but inhibit catalysis. Thus, the competition between Mg2+ and Ca2+ for a given metal-binding site in an enzyme and their effects on enzyme activity are of great interest. Most studies have focused on the interactions between Mg2+ or Ca2+ and the metal ligands in the first and sometimes second coordination shell.