Molecular dynamics of a cytochrome c-cytochrome b5 electron transfer complex

Cytochrome c and cytochrome b5 form an electrostatically associated electron transfer complex. Computer models of this and related complexes that were generated by docking the x-ray structures of the individual proteins have provided insight into the specificity and mechanism of electron transfer reactions. Previous static modeling studies were extended by molecular dynamics simulations of a cytochrome c-cytochrome b5 intermolecular complex. The simulations indicate that electrostatic interactions at the molecular interface results in a flexible association complex that samples alternative interheme geometries and molecular conformations. Many of these transient geometries appear to be more favorable for electron transfer than those formed in the initial model complex. Of particular interest is a conformational change that occurred in phenylalanine 82 of cytochrome c that allowed the phenyl side chain to bridge the two cytochrome heme groups.     

Protein crystal growth in microgravity

The crystals of most proteins or other biological macromolecules are poorly ordered and diffract to lower resolutions than those observed for most crystals of simple organic and inorganic compounds. Crystallization in the microgravity environment of space may improve crystal quality by eliminating convection effects near growing crystal surfaces. A series of 11 different protein crystal growth experiments was performed on U.S. space shuttle flight STS-26 in September 1988. The microgravity-grown crystals of gamma-interferon D1, porcine elastase, and isocitrate lyase are larger, display more uniform morphologies, and yield diffraction data to significantly higher resolutions than the best crystals of these proteins grown on Earth.     

Liquid chromatographic determination of basic nitrogen-containing polynuclear aromatic hydrocarbons in smoked foods

Several smoked foods were analyzed for basic nitrogen-containing polynuclear aromatic hydrocarbon (NPAH) content by a relatively rapid liquid chromatographic (LC) technique. The analyzed products included both domestic and imported market basket commodities. Nanogram quantities of NPAH standards were detected by UV and fluorescence detectors connected in series. The NPAHs were extracted from basic aqueous ethanolic solution into cyclohexane, extracted from cyclohexane into 6N HCl, and extracted back into cyclohexane after neutralization of the acid. The NPAHs were then purified by filtering the extract through deactivated basic alumina. The eluate from this step was concentrated to dryness, and the residue was dissolved in 95% ethanol and analyzed by LC, using a Vydac C-18 column and acetonitrile-water (9 + 1) as the mobile phase. Recoveries of 3 NPAHs, 5,7-dimethylbenz(a)acridine, dibenz(a,j)acridine, and dibenz(a,h)acridine, each added to salmon and sausage at the 5 ppb level, ranged from 62 to 101% by fluorescence measurement and from 64 to 106% by UV measurement. None of the NPAHs used as standards were found by either fluorescence or UV detection at levels greater than or equal to 5 ppb in any of the foods analyzed.     

Structural origins of high-affinity biotin binding to streptavidin

The high affinity of the noncovalent interaction between biotin and streptavidin forms the basis for many diagnostic assays that require the formation of an irreversible and specific linkage between biological macromolecules. Comparison of the refined crystal structures of apo and a streptavidin:biotin complex shows that the high affinity results from several factors. These factors include the formation of multiple hydrogen bonds and van der Waals interactions between biotin and the protein, together with the ordering of surface polypeptide loops that bury the biotin in the protein interior. Structural alterations at the biotin binding site produce quaternary changes in the streptavidin tetramer. These changes apparently propagate through cooperative deformations in the twisted beta sheets that link tetramer subunits.     

Electrochemotherapy for the treatment of recurring aponeurotic fibromatosis in a dog

This paper reports the clinical findings, histopathology, and clinical outcome of a rare case of aponeurotic fibromatosis in a dog. The dog was treated with 4 courses of electrochemotherapy using the drugs cisplatin and bleomycin. There was complete remission and the dog was still disease-free after 18 months.