Book review

Ernest R. Alexander Published by Gordon and Breach Publishers, Amsterdam, Holland 1995. 355 pages. ISBN 2-88449-173-2     

Colored plasmons in a quark-gluon plasma near equilibrium

Within a kinetic theory for QCD plasmas we study the color response function near thermodynamic equilibrium. Its poles yield a longitudinal and a transverse collective mode, both starting at the plasma frequency. Due to the gluon contribution there is no Landau damping for these modes, and creation of gluon or q-$\text{p}$ pairs is the dominant damping mechanism. In an electron plasma the generally quoted Landau damping near threshold is shown to be an artifact of the non-relativistic approximation.     

A novel SRN1 substitution: the reaction between the anion of 2-nitropropane and 3-bromo-1-nitrocyclohex-1-ene

X-Ray crystallography has been used to determine the unusual cyclopropyl structure for the product of the S_RNl reaction between the anion of 2-nitropropane and 3-bromo-1-nitrocyclohex-1-ene.     

Direct synthesis of pyran-lactones related to naphthoquinoneantibiotics

Simple benzopyrans with a fused γ-lactone unit are prepared from an o-disubstituted arene by direct intramolecular alkoxycarbonylation/lactonization promoted by palladium diacetate; the process gives high yields and moderate stereoselectivity, favoring the $\text{cis}$ lactone over $\text{trans}$ by a factor of 5:1.     

On optimal embeddings of metrics in graphs

This paper extends previous results of the authors. In particular, non-treerealizable metrics are investigated and it is shown that every finite metric has an optimal realization by a graph.     

Enamine carboxylates as stereodetermining intermediates in prolinate catalysis

Experimental and computational studies probing the nature of intermediates in the α-amination of aldehydes catalyzed by prolinate salts support an enamine carboxylate intermediate in the stereodetermining step.     

N-terminal protein modification using simple aminoacyl transferase substrates

Methods for synthetically manipulating protein structure enable greater flexibility in the study of protein function. Previous characterization of the Escherichia coli aminoacyl tRNA transferase (AaT) has shown that it can modify the N-terminus of a protein with an amino acid from a tRNA or a synthetic oligonucleotide donor. Here, we demonstrate that AaT can efficiently use a minimal adenosine substrate, which can be synthesized in one to two steps from readily available starting materials. We have characterized the enzymatic activity of AaT with aminoacyl adenosyl donors and found that reaction products do not inhibit AaT. The use of adenosyl donors removes the substrate limitations imposed by the use of synthetases for tRNA charging and avoids the complex synthesis of an oligonucleotide donor. Thus, our AaT donors increase the potential substrate scope and reaction scale for N-terminal protein modification under conditions that maintain folding.