muramidase and farrerol

muramidase has been researched along with farrerol* in 1 studies

Other Studies

1 other study(ies) available for muramidase and farrerol

ArticleYear
Binding analysis of farrerol to lysozyme by spectroscopic methods.
    Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy, 2007, Volume: 68, Issue:2

    Binding of farrerol to lysozyme (LYSO) was investigated at 302, 313 and 318 K at pH 7.4 using spectrophotometric techniques such as fluorescence emission, circular dichroism (CD) and UV absorption. The data obtained from fluorescence quenching experiments showed that farrerol was bound to LYSO and the affinity was enhanced by the addition of farrerol. When the concentration ratio of farrerol to LYSO was higher than 5.4, both the binding constant and the binding stoichiometry went up. Based on the thermodynamic parameters evaluated from the van't Hoff equation, the enthalpy change (deltaH degrees ) and entropy change (deltaS degrees ) were derived to be negative values. They indicated that both van der Waals forces and hydrogen bonds are the major interactions between farrerol and LYSO. A value of 2.67 nm for the average distance r between farrerol (acceptor) and tryptophan residues (Trp) of LYSO (donor) was derived from the fluorescence resonance energy transfer. Besides, the change in the conformation of LYSO was observed, being caused by the interaction with farrerol.

    Topics: Animals; Binding Sites; Chromones; Circular Dichroism; Hydrogen Bonding; In Vitro Techniques; Kinetics; Muramidase; Protein Conformation; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Thermodynamics; Tryptophan

2007