A six-dimensional quadrature procedure

An account is given of the use of Gaussian quadrature product formulae in the evaluation of certain six-dimensional, two-centre integrals involving one-electron Green's functions. These integrals occur in a new molecular variational principle recently proposed by Hall, Hyslop and Rees [1] from which an approximate energy may be derived which can be shown to be at least as good as that obtained from the Rayleigh-Ritz principle. Reductions in computing time are realized by removing certain singularities using a subtraction technique and also by using an empirically determined Richardson-type extrapolation formula.This paper was presented during the session on numerical integration methods for molecules of the 1970 Quantum Theory Conference in Nottingham. It has been revised in the light of the interesting discussion which followed.     

MRI findings of primary small-cell carcinoma of kidney

We report the MRI findings of primary small-cell carcinoma of the kidney (PSCCK) in a 59-year-old female. This tumor appeared as a 16-cm mass that arose from the right kidney. This lesion had diminished signal on T1-weighted images and heterogeneous mixed signal on T2-weighted images. The tumor primarily involved the renal medulla with persistent thin renal cortex. Despite the tumors' large size, no substantial central necrosis was present. The predominant medullary location and the lack of central necrosis in this large tumor were features unusual for renal cell carcinoma and should raise the suspicion of another malignancy, the differential diagnosis of which should contain extrapulmonary small-cell carcinoma of the kidney.     

Femtomolar Zn(II) affinity in a peptide-based ligand designed to model thiolate-rich metalloprotein active sites

Metal-ligand interactions are critical components of metalloprotein assembly, folding, stability, electrochemistry, and catalytic function. Research over the past 3 decades on the interaction of metals with peptide and protein ligands has progressed from the characterization of amino acid-metal and polypeptide-metal complexes to the design of folded protein scaffolds containing multiple metal cofactors. De novo metalloprotein design has emerged as a valuable tool both for the modular synthesis of these complex metalloproteins and for revealing the fundamental tenets of metalloprotein structure-function relationships. Our research has focused on using the coordination chemistry of de novo designed metalloproteins to probe the interactions of metal cofactors with protein ligands relevant to biological phenomena. Herein, we present a detailed thermodynamic analysis of Fe(II), Co(II), Zn(II), and[4Fe-4S]2(+/+) binding to IGA, a 16 amino acid peptide ligand containing four cysteine residues, H2N-KLCEGG-CIGCGAC-GGW-CONH2. These studies were conducted to delineate the inherent metal-ion preferences of this unfolded tetrathiolate peptide ligand as well as to evaluate the role of the solution pH on metal-peptide complex speciation. The [4Fe-4S]2(+/+)-IGA complex is both an excellent peptide-based synthetic analogue for natural ferredoxins and is flexible enough to accommodate mononuclear metal-ion binding. Incorporation of a single ferrous ion provides the FeII-IGA complex, a spectroscopic model of a reduced rubredoxin active site that possesses limited stability in aqueous buffers. As expected based on the Irving-Williams series and hard-soft acid-base theory, the Co(II) and Zn(II) complexes of IGA are significantly more stable than the Fe(II) complex. Direct proton competition experiments, coupled with determinations of the conditional dissociation constants over a range of pH values, fully define the thermodynamic stabilities and speciation of each MII-IGA complex. The data demonstrate that FeII-IGA and CoII-IGA have formation constant values of 5.0 x 10(8) and 4.2 x 10(11) M-1, which are highly attenuated at physiological pH values. The data also evince that the formation constant for ZnII-IGA is 8.0 x 10(15) M-1, a value that exceeds the tightest natural protein Zn(II)-binding affinities. The formation constant demonstrates that the metal-ligand binding energy of a ZnII(S-Cys)4 site can stabilize a metalloprotein by -21.6 kcal/mol. Rigorous thermodynamic analyses such as those demonstrated here are critical to current research efforts in metalloprotein design, metal-induced protein folding, and metal-ion trafficking.     

Unsupported lead clusters and electron diffraction

A beam of Pb clusters is produced with the inert gas aggregation method and probed by electron diffraction. Analysis of the diffraction patterns indicates that average cluster size can vary between 3 and 7 nm, according to nucleation conditions. The diffraction patterns from beams with larger average cluster size are very similar to patterns calculated from model decahedron clusters, while those for smaller cluster size do not appear to have simple geometrical face-centred cubic, decahedral, or icosahedral structure. Received 30 November 2000     

A numerical integration scheme for iterative calculations on atomic systems

A recursive numerical integration scheme based on the method of Clenshaw and Curtis is proposed for the efficient implementation of the variation–iteration procedure for the computation of approximate energies and wave functions for atomic systems. Extensive numerical tests are carried out to assess the accuracy and efficiency of the method and inaccuracies in some earlier calculations are pointed out.     

A minimum principle for molecular systems allowing the use of discontinuous wave functions

In this paper the minimum principle proposed for atomic systems by Hall, Hyslop and Rees [1] is generalized to molecules. It is shown that this generalization retains the advantage of admitting the use of a larger class of trial wave functions, for example those with discontinuities, than is possible in the usual minimum energy principle. The further advantage that the upper bounds obtained by this treatment are always at least as good as those of the Rayleigh-Ritz method is also preserved. The theory is applied to the H ion, potential energy curves are obtained for various “cut-off” wave functions, and the equilibrium internuclear distance is calculated. The optimization of the “cut-off” region so that the upper bound is minimized is also discussed.     

Purification and initial characterization of a novel protein with factor Xa activity from Lonomia obliqua caterpillar spicules

A novel protein with factor Xa-like activity was isolated from Lonomia obliqua caterpillar spicules by gel filtration chromatography and reversed-phase high-performance liquid chromatography. The protein had a mass of 20745.7 Da, as determined by mass spectrometry, and contained four Cys residues. Enzymatic hydrolysis followed by de novo sequencing by tandem mass spectrometry was used to determine the primary structure of the protein and the cysteine residues linked by disulfide bridges. The positions of 24 sequenced tryptic peptides, including the N-terminal, were deduced by comparison with a homologous protein from the superfamily Bombycoidea. Approximately 90% of the primary structure of the active protein was determined.