Interaction of Hydrophobic Molecules with Heme Proteins
Abstract
This research project investigated the effects of hydrophobic molecules on the structure and function of proteins. Proteins have hydrophobic interior regions where interaction with hydrophobic molecules may occur. The amino acid residues concerned with the active site and the binding of prosthetic groups are evolutionarily conserved. In general, the hydrophobic residues in proteins are also conserved, although not highly (ie., a hydrophobic residue, perhaps not the same identical residue, is usually present at a certain position in the protein). This evolutionary conservation indicates the importance of the hydrophobic interior to the maintenance of the three dimensional protein structure and hence its function. Perturbation of the hydrophobic region can be expected to alter structure/function, particularly in heme proteins, where the heme prosthetic groups lies in a hydrophobic pocket or region. Proteins that are integral components of membranes have an additional hydrophobic region on the surface of the protein where interaction with the membrane lipids occurs. Integral proteins such as cytochrome oxidase, will have a hydrophobic protein interior as well as an exterior surface where 45-50 'boundary' or interfacial lipids are found. In these integral proteins, conformation and enzymatic activity are dependent on lipid; depletion or exchange of lipid by another type result in decreased activity. Thus, perturbation of the hydrophobic surface of integral proteins may also alter structure/function. Keywords: Reaction kinetics, Molecule molecule interactions, Active site, Binding site.
Document Details
- Document Type
- Technical Report
- Publication Date
- Aug 29, 1988
- Accession Number
- ADA198747
Entities
People
- H. J. Harmon
Organizations
- Oklahoma State University–Stillwater