Correction to: Involutions of Type G2 over a Field of Characteristic Two

Algebras and Representation Theory - We would like to correct two errors in our paper Involutions of type G2 over a field of characteristic 2 [2].     

Magnetic properties of Ln3In intermetallic compounds

Results of magnetic studies of Ln₃In phases (Ln = Pr, Nd, Gd, Dy and Er) are presented. All materials exhibited Curie-Weiss behavior in the paramagnetic regions with effective moments approximating $\text{g[J(J + 1)]}{}^{\mathrm{<mtext>1</mtext><mtext>2</mtext>}}$ for the tripositive ion. Positive Weiss constants were observed indicating predominance of ferromagnetic exchange. Pr₃In and Nd₃In order ferromagnetically at 62 and 114 K, respectively. However, the ordered moment is less than 10% of gJ. Dy₃In and Er₃In also seem to order ferromagnetically, but with low moments compared to gJ. Gd₃In exhibits metamagnetic behavior with a critical field of about 5 kOe. Neutron diffraction measurements on Nd₃In indicate that it is ferromagnetic and confirm the low Nd³⁺ moment.     

Differences in the conformational state of a zinc-finger DNA-binding protein domain occupied by zinc and copper revealed by electrospray ionization mass spectrometry.

Transition metal ions are important in biological regulation partly because they can bind to and stabilize protein surface domain structures in specific conformations that are involved in key molecular recognition events. There are two C2-C2 type zinc-finger sequences within the highly conserved DNA-binding domain of the estrogen receptor protein (ERDBD). Electrospray ionization (ESI) mass spectrometry has been used to demonstrate that the metal-binding sites within the 71-residue ERDBD can bind either Zn (up to 2) or Cu (up to 4). Evidence for the induction and/or stabilization of a different conformational state with bound Cu is revealed by a characteristic shift in the ESI charge envelope. The 10+ charge state is most abundant for the fully reduced ERDBD apopeptide and the ERDBD-Zn holopeptide (bound Zn does not alter the charge envelope). In contrast, the 8+ charge state is typically the optimum charge state observed for the ERDBD-Cu holopeptide; indeed, the entire charge envelope is frame-shifted to lower charge states with bound Cu. Interpretation of the altered charge states is simplified because (i) a single type of metal-binding ligand (sulfur) is involved in the case of both Zn and Cu binding, and (ii) the two different metal cations are both divalent. Thus, it is likely that the dissimilar charge envelopes represent different peptide conformers, each of which is stabilized by a different type of bound metal ion.(ABSTRACT TRUNCATED AT 250 WORDS)     

Analysis of uniaxial compression of vertically aligned carbon nanotubes

We carry out axisymmetric, finite deformation finite element analyses of the uniaxial compression of cylindrical bundles of vertically aligned carbon nanotubes (VACNTs) firmly attached to a Si substrate. A compressible elastic–viscoplastic constitutive relation with a piecewise, linear hardening–softening–hardening flow strength is used to model the material. Calculations are performed for VACNTs both with uniform properties and with axially graded properties. We show that, with uniform properties, sequential buckling initiates at the substrate and propagates away from it, in agreement with previous experimental findings. We investigate the dependence of the magnitude and wavelength of the buckles on characteristics of the function defining the flow strength. When a property gradient giving a more compliant response at the end opposite to the substrate is specified, we find that sequential buckling initiates at that end and propagates toward the substrate. Results of the analyses are compared with the experimental observations and capture many of the experimentally obtained stress–strain and morphological features. The proposed model serves as a promising foundation for capturing the underlying energy absorption mechanisms in these systems. Comparison of the model predictions with the experimental results also suggests directions for model improvement.     

Metal ligand-induced alterations in the surface structures of lactoferrin and transferrin probed by interaction with immobilized copper(II) ions

We have evaluated immobilized Cu(II) ions as a potential site-directed molecular probe to monitor ligand-induced alterations in protein surface structures. Metal ion-induced alterations in the surface structures of different lactoferrins (human and porcine), transferrins (human and rabbit), and ovotransferrin (chicken) were examined. Although these 78,000-dalton glycoproteins are related gene products with similar overall structure and function, they differ greatly in the number and distribution of surface-exposed electron-donor groups thought to interact with Cu(II) ions. Each of these proteins interacted with immobilized Cu(II) ions through sites which are distinct from the two specific high affinity metal binding sites identified for iron. In both the presence and absence of bound iron, transferrins interacted more strongly with the immobilized Cu(II) ions than did lactoferrins; ovotransferrin interacted only weakly. Although iron binding increased the affinities of lactoferrins for immobilized Cu(II), iron binding decreased the affinities of transferrins and ovotransferrin for immobilized Cu(II) ions. Iron-saturated and iron-free lactoferrins were resolved by pH gradient elution, but only in the presence of 3 M urea; they were not resolved by imidazole affinity elution. Conversely, the iron-saturated and iron-free forms of transferrin were only separated by imidazole affinity elution. Urea did not influence the resolution of apo and holo ovotransferrins by imidazole. The differential effects of urea and imidazole suggest the participation of different types of surface electron-donor groups. The progressive site-specific modification of surface-exposed histidyl residues by carboxyethylation revealed several lactoferrin forms of intermediate affinity for immobilized iminodiacetate-Cu(II) ions. In summary, independent of species, the affinity for immobilized Cu(II) ions increased as follows: iron-saturated ovotransferrin less than metal-free ovotransferrin less than apolactoferrin less than hololactoferrin much less than diferric or holotransferrin less than monoferric transferrin less than apotransferrin. We have demonstrated the use of immobilized Cu(II) ions to distinguish and to monitor ligand-induced alterations in protein surface structure. The results are discussed in relation to protein surface-exposed areas of electron-donor groups.     

Deformation of plastically compressible hardening-softening-hardening solids

Motivated by a model of the response of vertically aligned carbon nanotube (VACNT) pillars in uniaxial compression, we consider the deformation of a class of compressible elastic-viscoplastic solids with a hardening-softening-hardening variation of flow strength with plastic strain. In previous work (Hutchens et al. 2011) a constitutive relation was presented and used to model the response of VACNT pillars in axisymmetric compression. Subsequently, it was found that due to a programming error the constitutive relation presented in the paper (Hutchens et al. 2011) was not the one actually implemented. In particular, the plastic flow rule actually used did not satisfy plastic normality. Here, we present the constitutive formulation actually implemented in the previous work (Hutchens et al. 2011). Dynamic, finite deformation, finite element calculations are carried out for uniaxial compression, uniaxial tension and for indentation of a "half-space" by a conical indenter tip. A sequential buckling-like deformation mode is found in com- pression when there is plastic non-normality and hardening-softening-hardening. The same material characterization gives rise to a Lüders band-like deformation mode in ten- sion. When there is a deformation mode with a sharp front along mesh boundaries, the overall stress-strain response contains high frequency oscillations that are a mesh artifact. The responses of non-softening solids are also analyzed and their overall stress-strain behavior and deformationmodes are compared with those of hardening-softening- hardening solids. We find that indentation with a sharp in- denter tip gives a qualitatively equivalent response for hardening and hardening-softening-hardening solids.     

Synthetic metal-binding protein surface domains for metal ion-dependent interaction chromatography. II. Immobilization of synthetic metal-binding peptides from metal ion transport proteins as model bioactive protein surface domains.

This preliminary investigation tests the premise that biologically relevant (1) peptide-metal ion interactions, and (2) metal ion-dependent macromolecular recognition events (e.g., peptide-peptide interactions) may be modeled by biomimetic affinity chromatography. Divinylsulfone-activated agarose (6%) was used to immobilize three different synthetic peptides representing metal-binding protein surface domains from the human plasma metal transport protein histidine-rich glycoprotein (HRG). The synthetic peptides represented 1-3 multiple repeat units of the 5-residue sequence (Gly-His-His-Pro-His) found in the C-terminal of HRG. By frontal analyses, immobilized HRG peptides of the type (GHHPH)nG, where n = 1-3, were each found to have a similar binding capacity for both Cu(II) ions and Zn(II) ions (31-38 mumol/ml gel). The metal ion-dependent interaction of a variety of model peptides with each of the immobilized HRG peptide affinity columns demonstrated differences in selectivity despite the similar internal sequence homology and metal ion binding capacity. The immobilized 11-residue HRG peptide was loaded with Cu(II) ions and used to demonstrate selective adsorption and isolation of proteins from human plasma. These results suggest that immobilized metal-binding peptides selected from known solvent-exposed protein surface metal-binding domains may be useful model systems to evaluate the specificity of biologically relevant metal ion-dependent interaction and transfer events in vitro.