Jeremy Kua

Summary

Affiliation: University of California
Country: USA

Publications

  1. ncbi request reprint Studying enzyme binding specificity in acetylcholinesterase using a combined molecular dynamics and multiple docking approach
    Jeremy Kua
    Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla, California 92093 0365, USA
    J Am Chem Soc 124:8260-7. 2002
  2. pmc Studying the roles of W86, E202, and Y337 in binding of acetylcholine to acetylcholinesterase using a combined molecular dynamics and multiple docking approach
    Jeremy Kua
    Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla, California 92093, USA
    Protein Sci 12:2675-84. 2003
  3. ncbi request reprint Role of the catalytic triad and oxyanion hole in acetylcholinesterase catalysis: an ab initio QM/MM study
    Yingkai Zhang
    Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla, California 92093 0365, USA
    J Am Chem Soc 124:10572-7. 2002
  4. ncbi request reprint Molecular docking of balanol to dynamics snapshots of protein kinase A
    Chung F Wong
    Department of Chemistry and Biochemistry, University of Missouri St Louis, Missouri 63121, USA
    Proteins 61:850-8. 2005
  5. doi request reprint Glycolaldehyde monomer and oligomer equilibria in aqueous solution: comparing computational chemistry and NMR data
    Jeremy Kua
    Department of Chemistry and Biochemistry, University of San Diego, 5998 Alcala Park, San Diego, California 92110, USA
    J Phys Chem A 117:2997-3008. 2013
  6. ncbi request reprint Thermodynamics and kinetics of methylboroxine.amine adduct formation: a computational study
    Jeremy Kua
    Department of Chemistry, University of San Diego, 5998 Alcala Park, San Diego, California 92110, USA
    J Phys Chem A 111:4759-66. 2007
  7. ncbi request reprint Computational study of multiple-decker sandwich and rice-ball structures of neutral titanium-benzene clusters
    Jeremy Kua
    Department of Chemistry, University of San Diego, 5998 Alcala Park, San Diego, California 92110, USA
    J Phys Chem A 110:11988-94. 2006

Detail Information

Publications7

  1. ncbi request reprint Studying enzyme binding specificity in acetylcholinesterase using a combined molecular dynamics and multiple docking approach
    Jeremy Kua
    Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla, California 92093 0365, USA
    J Am Chem Soc 124:8260-7. 2002
    ..Substituting each tail methyl group with hydrogen results in both an incremental loss in docking energy and also a decrease in the percentage of structures docked in the active site correctly set up for catalysis...
  2. pmc Studying the roles of W86, E202, and Y337 in binding of acetylcholine to acetylcholinesterase using a combined molecular dynamics and multiple docking approach
    Jeremy Kua
    Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla, California 92093, USA
    Protein Sci 12:2675-84. 2003
    ..We also find that all perturbations result in a significant reduction in binding of extended ACh in the catalytically productive orientation. This effect is primarily caused by a small shift in preferred position of the quaternary tail...
  3. ncbi request reprint Role of the catalytic triad and oxyanion hole in acetylcholinesterase catalysis: an ab initio QM/MM study
    Yingkai Zhang
    Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla, California 92093 0365, USA
    J Am Chem Soc 124:10572-7. 2002
    ..As the reaction proceeds, the distance between the carbonyl oxygen of ACh and NH group of Ala204 becomes smaller, and the third hydrogen bond is formed both in the transition state and in the tetrahedral intermediate...
  4. ncbi request reprint Molecular docking of balanol to dynamics snapshots of protein kinase A
    Chung F Wong
    Department of Chemistry and Biochemistry, University of Missouri St Louis, Missouri 63121, USA
    Proteins 61:850-8. 2005
    ..We found that a useful way to identify the correctly docked structure was to locate the structure that appeared most frequently as the lowest energy structure in the docking experiments to different snapshots...
  5. doi request reprint Glycolaldehyde monomer and oligomer equilibria in aqueous solution: comparing computational chemistry and NMR data
    Jeremy Kua
    Department of Chemistry and Biochemistry, University of San Diego, 5998 Alcala Park, San Diego, California 92110, USA
    J Phys Chem A 117:2997-3008. 2013
    ....
  6. ncbi request reprint Thermodynamics and kinetics of methylboroxine.amine adduct formation: a computational study
    Jeremy Kua
    Department of Chemistry, University of San Diego, 5998 Alcala Park, San Diego, California 92110, USA
    J Phys Chem A 111:4759-66. 2007
    ..amine adduct and find that the pathway is most likely similar, except that the transformation is thermodynamically and kinetically more favored for the phenyl system in the presence of pyridine...
  7. ncbi request reprint Computational study of multiple-decker sandwich and rice-ball structures of neutral titanium-benzene clusters
    Jeremy Kua
    Department of Chemistry, University of San Diego, 5998 Alcala Park, San Diego, California 92110, USA
    J Phys Chem A 110:11988-94. 2006
    ..The larger rice-ball structures, on the other hand, preferred to weaken the metal-metal bonds and retain eta(6)-Bz bound to a single metal atom, a structural motif shared with sandwiches...