Abstract
An approach to a quantitative experimental description of enzyme denaturations is considered. A parameter, Ω, derived from the first moment of the aromatic region of ribonuclease A nuclear magnetic resonance spectra, is used to follow thermal and lithium bromide denaturations. It is shown that Ω does not depend on widths of individual resonance lines; consequently, it can be defined from even poorly resolved protein spectra. The parameter Ω permits one to follow protein denaturations as shown by a well-defined number of aromatic residues. An interpretation of Ω is given assuming that a protein denaturation, like a homopolypeptide denaturation, is a continuous process within each macromolecule.
Published Version
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