Thermochemistry of Lysozyme-Inhibitor Binding

Influence of inhibitor binding on the internal motions of lysozyme.

Time-resolved laser-induced fluorescence depolarization measurements of internal motions in lysozyme are presented. The fluorescent dye eosin binds in a one-to-one complex with the enzyme, and is used both to measure the overall tumbling time constants and to probe the motions of residues in the region of binding. The precision and accuracy of the present method for determining the overall tumb...

Binding with lysozyme of antibodies against surface-simulation peptides representing the lysozyme antigenic sites.

Previously it had been shown that native lysozyme has three discontinuous antigenic sites (comprising spatially adjacent residues that may be distant in sequence) that were mimicked by surface-simulation synthetic peptides that had the capacity to bind the bulk (97-99%) of the antibody response against native lysozyme. In the present work these three surface-simulation synthetic peptides were c...

Inhibitor Binding

An inhibitor was isolated from the maternal part of bovine p l a c e n t a s which inhibits the incorporation of [ 3 H ] t h y m i d i n e into the DNA of a variety of tumor ceils to a significantly higher degree as compared to normal cells. This protein-type component was labeled by reaction with N-succinimidyl[2,3-3H]propionate, and i n t e r a c t i o n s with receptors on cell membranes wer...

Protein normal-mode dynamics: trypsin inhibitor, crambin, ribonuclease and lysozyme.

We have developed a new method for modelling protein dynamics using normal-mode analysis in internal co-ordinates. This method, normal-mode dynamics, is particularly well suited for modelling collective motion, makes possible direct visualization of biologically interesting modes, and is complementary to the more time-consuming simulation of molecular dynamics trajectories. The essential assump...

Effect of antibody binding on the mobility of serum lysozyme.