A specific temperature-dependent conformational transition of hen egg-white lysozyme, occurring between 20 degree C and 30 degree C in solution, has been detected by 13-C-nuclear magnetic resonance spectroscopy. Selective changes in the chemical shifts of aromatic residues, together with differences in the chemical shifts, and nuclear Overhauser enhancement in the carbonyl, carboxyl, and alpha-...

The binding of beta-methyl N-acetylglucosaminide (betaMeGlcNAc) to egg-white lysozyme of hen in the tetragonal crystal form was studied by X-ray diffraction techniques to a resolution of 0.25 nm. The binding of the beta-methyl glycoside is almost identical with the binding of beta-N-acetylglucosamine (betaGlcNAc). Real-space refinement of the lysozyme-alpha/beta GlcNAc and lysozyme-betaMeGlcNAc...

abstractinteraction of ni complex(salen= n, n´-ethylene bis(salicylideneimine)) with hen egg-white lysozyme (hewl) was studied by absorption spectroscopy, competitive binding study and thermal denaturation study. the protein binding affinity of ni complex was found to be (3.0×103m−1). the binding plot obtained from the absorption titration data gives a binding constant of 2.4 (± 0.3)×103 m-1. i...