Johns Hopkins University-ko ikertzaileekin lankidetzan egindako argitalpenak (7)

2001

  1. Enzyme kinetics determined using calorimetry: A general assay for enzyme activity?

    Analytical Biochemistry, Vol. 296, Núm. 2, pp. 179-187

1998

  1. Molecular basis of resistance to HIV-1 protease inhibition: A plausible hypothesis

    Biochemistry, Vol. 37, Núm. 17, pp. 5791-5797

  2. Structural thermodynamic study of the binding of renin inhibitors to endothiapepsin

    Advances in Experimental Medicine and Biology

  3. Structure-based thermodynamic design of peptide ligands: Application to peptide inhibitors of the aspartic protease endothiapepsin

    Proteins: Structure, Function and Genetics, Vol. 30, Núm. 1, pp. 74-85

1996

  1. The enthalpy change in protein folding and binding: Refinement of parameters for structure-based calculations

    Proteins: Structure, Function and Genetics, Vol. 26, Núm. 2, pp. 123-133

  2. The magnitude of the backbone conformational entropy change in protein folding

    Proteins: Structure, Function and Genetics, Vol. 25, Núm. 2, pp. 143-156

1995

  1. The heat capacity of proteins

    Proteins: Structure, Function, and Bioinformatics, Vol. 22, Núm. 4, pp. 404-412