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1.
Bioorg Med Chem Lett ; 10(21): 2427-30, 2000 Nov 06.
Article in English | MEDLINE | ID: mdl-11078193

ABSTRACT

Isothermal titration calorimetry was used to analyze the binding of an enantiomeric pair of inhibitors to the stromelysin-1 catalytic domain. Differences in binding affinity are attributable to different conformational entropy penalties suffered upon binding. Two possible explanations for these differences are proposed.


Subject(s)
Hydroxamic Acids/chemistry , Hydroxamic Acids/metabolism , Matrix Metalloproteinase Inhibitors , Oligopeptides/chemistry , Oligopeptides/metabolism , Protease Inhibitors/chemistry , Protease Inhibitors/metabolism , Calorimetry/methods , Catalytic Domain , Humans , Matrix Metalloproteinase 3/metabolism , Molecular Conformation , Molecular Structure , Protein Binding , Stereoisomerism , Thermodynamics
2.
Proteins ; Suppl 2: 28-37, 1998.
Article in English | MEDLINE | ID: mdl-9849908

ABSTRACT

Mass spectrometry (MS) with electrospray ionization (ESI) has shown utility for studying noncovalent protein complexes, as it offers advantages in sensitivity, speed, and mass accuracy. The stoichiometry of the binding partners can be easily deduced from the molecular weight measurement. In many examples of protein complexes, the gas phase-based measurement is consistent with the expected solution phase binding characteristics. This quality suggests the utility of ESI-MS for investigating solution phase molecular interactions. Complexes composed of proteins from the human immunodeficiency virus (HIV) have been studied using ESI-MS. Multiply charged protein dimers from HIV integrase catalytic core (F185K) and HIV protease have been observed. Furthermore, the ternary complex between HIV protease dimer and inhibitor pepstatin A was studied as a function of solution pH. Zinc binding to zinc finger-containing nucleocapsid protein (NCp7) and the NCp7-psi RNA 1:1 stoichiometry complex was also studied by ESI-MS. No protein-RNA complex was observed in the absence of zinc, consistent with the role of the zinc finger motifs for RNA binding.


Subject(s)
Capsid Proteins , Capsid/metabolism , Gene Products, gag/metabolism , HIV Integrase/metabolism , HIV Protease/metabolism , Viral Proteins , Zinc Fingers , Amino Acid Sequence , Capsid/chemistry , Dimerization , Gene Products, gag/chemistry , HIV Integrase/chemistry , HIV Protease/chemistry , HIV Protease Inhibitors/metabolism , Humans , Mass Spectrometry , Molecular Sequence Data , Pepstatins/metabolism , RNA/metabolism , Zinc/metabolism , gag Gene Products, Human Immunodeficiency Virus
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