Prediction and understanding of the folding and stability of the 3D struc-ture of proteins is still a challenge. The different atomic interactions, such as non polar contacts and hydrogen bonding, are known but their exact relative weights and roles when contributing to protein folding and stability are not identified.
The role of the two disulfide bonds (Cys4–Cys60 and Cys18–Cys29) in the
activity and stability of goose-type (G-type) lysozyme was investigated
using ostrich egg-white lysozyme as a model. Each of the two disulfide
bonds was deleted separately or simultaneously by substituting both Cys
residues with either Ser or Ala.
We have reported previously that the calcium-depleted form of bovine
a-lactalbumin (apoa-LA) interacts with hen egg-white lysozyme (LYS) to
form spherical supramolecular structures. These supramolecular structures
contain an equimolar ratio of the two proteins. We further explore here
the organization of these structures.
The interaction of antibodies (Abs) with protein antigens (Ags) of different
size, such as hen egg white lysozyme, ovalbumin, and bovine serum albu-min, was examined using analytical ultracentrifugation, electrospray ioniza-tion time-of-flight mass spectrometry, and surface plasmon resonance in
order to estimate regional and segmental Ab flexibility.
One-electron oxidation of six different c-type lysozymes
from hen egg white, turkey egg white, human milk, horse
milk, camel stomach and tortoise was studied by gamma-and pulse-radiolysis.In the first step, one tryptophan side
chain is oxidized to indolyl free radical, which is produced
quantitatively.As shown already, the indolyl radical subse-quently oxidizes a tyrosine side chain to the phenoxy radical
in an intramolecular reaction.However this reaction is not
total and its stoichiometry depends on the protein.