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Crystallization of alloys from a molten state is a fundamental process underpinning metallurgy. Here the direct imaging of an intermetallic precipitation reaction at equilibrium in a liquid-metal environment is demonstrated. It is shown that the outer layers of a solidified intermetallic are surprisingly unstable to the depths of several nanometers, fluctuating between a crystalline and a liquid state. This effect, referred to herein as crystal interface liquefaction, is observed at remarkably low temperatures and results in highly unstable crystal interfaces at temperatures exceeding 200 K below the bulk melting point of the solid. In general, any liquefaction process would occur at or close to the formal melting point of a solid, thus differentiating the observed liquefaction phenomenon from other processes such as surface pre-melting or conventional bulk melting. Crystal interface liquefaction is observed in a variety of binary alloy systems and as such, the findings may impact the understanding of crystallization and solidification processes in metallic systems and alloys more generally., (© 2024 The Authors. Advanced Science published by Wiley‐VCH GmbH.)

The emergence of attractive properties in materials at atomically thin regimes has seen an ongoing interest in two-dimensional (2D) materials. An aspect that has lacked focused attention is the effect of 2D material thickness on its crystal structure. As several layered materials naturally exist in mixed metastable phases, it raises an important question of whether a specific polymorph of these mixed-phase materials will be favored at atomically thin limits. This work attempts to address this issue by employing lead monoxide as a model 2D polymorphic system. We propose a reactive oxygen species (ROS) sequestration-mediated liquid-phase exfoliation (LPE) strategy for the facile synthesis of ultrathin PbO. This is followed by a suite of microscopic and spectroscopic analyses of the PbO nanosheets that reveals the polymorphic transformation of orthorhombic (β) PbO to its tetragonal (α) analogue with reduction in nanosheet thickness. The transformation process reveals an interesting crystal structure of ultrathin 2D PbO where [001]-oriented domains of α-PbO coexist alongside [100]-oriented regions of β-PbO. Density functional theory (DFT) calculations support our experimental data by revealing a higher thermodynamic stability of the tetragonal phase in PbO monolayers. These findings are likely to instigate interest in carefully evaluating the crystal structures of ultrathin 2D materials while promoting research in understanding the phase transformation across a range of 2D crystals.

Single-atom and single-particle catalysis is an area of considerable topical interest due to their potential in explaining important fundamental processes and applications across several areas. An interesting avenue in single-particle catalysis is spatial control of chemical reactivity within the particle by employing light as an external stimulus. To demonstrate this concept, we report galvanic replacement reactions (GRRs) as a spatial marker of subparticle chemical reactivity of a silver nanoprism with AuCl 4 - ions under optical excitation. The location of a GRR within a single Ag nanoprism can be spatially controlled depending on the plasmon mode excited. This leads to chemomorphological transformation of Ag nanoprisms into interesting Ag-Au structures. This spatial biasing effect is attributed to localized hot electron injection from the tips and edges of the silver nanoprisms to the adjacent reactants that correlate with excitation of different surface plasmon modes. The study also employs low-energy-loss EELS mapping to additionally probe the spatially confined redox reaction within a silver nanoprism. The findings presented here allow the visualization of a plasmon-driven subparticle chemical transformation with high resolution. The selective optical excitation of surface plasmon eigenmodes of anisotropic nanoparticles offers opportunities to spatially modulate chemical transformations mediated by hot electron transfer.

An essential part of the characterization of any protein is the determination of its molecular weight. The method of choice for these determinations, because of its simplicity and rapidity, has most frequently been sodium dodecyl sulfate (SDS) gel electrophoresis (See Chapter 6 ). The alternative method of gel filtration under denaturing conditions (1,2) has not been so widely used, in part as a result of the longer times required for a single run. However, recent developments in gel filtration supports for high pressure liquid chromatography (HPLC) have made more rapid separations possible, and thus gel permeation HPLC is becoming a widely used technique for molecular weight determinations (3,4). Gel permeation HPLC, in addition to taking less time than SDS gel electrophoresis, allows easier quantitation and recovery of separated proteins, and the resolution is better than that achieved by gel filtration with conventional materials.

Reverse-phase high pressure liquid chromatography (HPLC) has proved to be an extremely versatile technique for rapid separation of peptides (reviewed in ref. 1). One of its uses is for peptide mapping, or "fingerprinting" (2-5) as an alternative procedure to the conventional two-dimensional separations on paper or thin-layer supports (See Chapter 21 ). Although the map obtained is one dimensional, the excellent resolving power of reverse-phase HPLC enables separation of the majority of peptides within a mixture. HPLC offers the advantages of high reproducibility, easy quantitation, and rapid analysis time, and is also suitable for automation.

A monoclonal antibody R1 against the human epidermal growth factor receptor has been used to study biosynthesis in the carcinoma cell line A431. Two glycoproteins of apparent mol. wts. 95 000 and 160 000 were immunoprecipitated from cells labelled for short times with [35S]methionine or [3H]mannose. Pulse-chase studies show the 160 000 mol. wt. glycoprotein to be a precursor of the 175 000 mol. wt. receptor, but do not establish a precursor role for the 95 000 mol. wt. glycoprotein. Limited proteolysis, peptide mapping, endoglycosidase digestion and the use of monensin and tunicamycin show that the 95 000 mol. wt. glycoprotein is structurally related to the 160 000 mol. wt. glycoprotein and that both glycoproteins have approximately 22 000 - 28 000 mol. wt. of oligosaccharide side chains. Monensin blocks conversion of the 160 000 to the 175 000 mol. wt. mature receptor, a process which involves complexing several of its N-linked oligosaccharide chains. Pulse-chase studies showed that an immunoprecipitable polypeptide of 115 000 mol. wt., or 95 000 mol. wt., in the presence of monensin, was secreted into the medium at late chase times. The possible mechanisms for the origins of all the receptor-related polypeptides are discussed.

Electrophoresis and chromatography on paper have proved extremely useful techniques for the separation of small peptides prior to amino acid sequencing. Polarity determines the rate of migration of a peptide during chromatography, whereas both charge and size are the main determinants during electrophoresis. The two techniques therefore are complimentary, and when used in conjunction can resolve most peptide mixtures into their pure components.

A survey of H1o and H5-like proteins has been conducted through a range of higher and lower eukaryotic species. All mammals examined possessed H1o proteins, although in variable amounts, and the protein's structure was well conserved, though not invariant. The testis-specific histone Hlt (from rat) did not have an H1o-like structure and it appears that H1o does not occur in spermatocytes in any form. The results also show that Xenopus laevis contains H1o-like proteins, but lower, non-vertebrate eukaryotes (a crustacean, two fungi and a plant tissue) do not possess H1o or H5 proteins. The evidence suggests that H1o and H5 proteins may be considered as belonging to one family, distinct from H1 types. This H1o/H5 family may well be 'replacement histone' variants of H1. The results do not support suggestions of roles such as repression of DNA synthesis or of transcription for H1o/H5 proteins.

Four proteins have been isolated from wheat germ by methods analogous to those used to isolate HMG proteins from animal tissue. All four proteins have been shown to be chromosomal in origin. Although amino acid analyses show that three of these proteins have compositions similar to those of the mammalian HMG proteins, N-terminal sequence analyses of these proteins show an absence of sequence homology with any of the mammalian HMG proteins.

Two proteins, HMG-T1 and HMG-T2, with electrophoretic mobilities and compositions similar to those of protein HMG-T, were isolated from trout testes nuclei. The isoelectric points of proteins HMG-T1, HMG-T2 and HMG-T differ. The first 20 residues of protein HMG-T2 have been sequenced and differ from protein HMG-T by only one residue.

The unique high specificity of antibodies, both polyclonal and monoclonal, makes them extremely valuable tools for rapid, selective purification of antigens. In principle, the antibody immobilized on a column support is used to selectively adsorb antigen from a mixture containing many other proteins (1,2). The other proteins, for which the antibody has no affinity, may be washed away, and the purified antigen then eluted from the immunoadsorbent. In order to dissociate the antigen from its high affinity antibody, the conditions for elution are necessarily extreme (1-3) and thus must be carefully chosen to permit isolation of active protein.

Hoggett & Kellett [Eur. J. Biochem. 66, 65-77 (1976)] have reported that the binding of glucose to the monomer of hexokinase PII isoenzyme is independent of ionic strength, in contrast to the subsequent claim of Feldman & Kramp [Biochemistry 17, 1541-1547 (1978)] that the binding is strongly dependent on ionic strength. Since measurements with native hexokinase P forms are complicated by the fact that the enzyme exists in a monomer-dimer association-dissociation equilibrium, we have now studied the binding of glucose to the proteolytically-modified S forms which are monomeric. At pH 8.5, the affinity of glucose for both SI and SII monomers is independent of salt concentration over the range of KCl concentrations 0-1.0 mol . dm-3 and is in good agreement with that of the corresponding P forms in both low and high salt. These observations confirm that the binding of glucose to hexokinase P monomers is independent of ionic strength and that the affinity of glucose for the hexokinase PII monomer is about an order of magnitude greater than that for the dimer.

A monoclonal antibody of the IgG class, EGFR1, has been isolated using cells of the epidermoid carcinoma line A431 as immunogen. The A431 antigen recognized by EGFR1 has an apparent molecular weight of approximately 175,000, is a cell-surface molecule which can be specifically cross-linked to EGF, exhibits an EGF-stimulated protein kinase activity, binds to EGFR1 in a number of human cell lines to a degree which parallels EGF binding, and shows EGF-dependent internalization in A431 cells and human fibroblasts. We therefore conclude that EGFR1 is directed against an antigenic site on the human EGF receptor. EGFR1 is not mitogenic for human fibroblasts and does not inhibit EGF binding under a variety of assay conditions. The characterization of EGFR1 has allowed the unambiguous assignment of the structural gene for the human EGF receptor to chromosome 7. Preliminary results suggest that a convenient method for isolating a range of anti-EGF receptor monoclonal antibodies can be developed, based on a hybridoma supernatant screening assay in which positive supernatants bind selectively to a human-mouse cell hybrid containing human chromosome 7.

A431 cells have been used as an immunogen for generating monoclonal antibodies against the epidermal growth factor (EGF) receptor. Two immunoglobulin M and eight immunoglobulin G3 anti-EGF receptor antibodies were cloned. All ten antibodies immunoprecipitated biosynthetically labeled mature A431 cell EGF receptor and were able to recognize the receptor in Western blotting. However, none of the antibodies immunoprecipitated precursor polypeptides of the A431 cell EGF receptor, neither did they recognize EGF receptors from human foreskin fibroblasts, human placenta, nor a human-mouse hybrid cell expressing EGF receptor. The antibodies were found to bind to glycolipids from A431 cells and it was shown that the determinant involved was the blood group A antigen. It appears that this determinant is present on both the EGF receptor and glycolipids of A431 cells but is not expressed on EGF receptors from other human cells tested. One of the monoclonal antibodies raised was used for immunoaffinity purification of the EGF receptor. The procedure took advantage of the carbohydrate nature of the antigenic determinant by employing sugar-specific elution. The mild conditions permitted the purification of A431 cell EGF receptor (70-80% pure) that possessed an intrinsic EGF-stimulated tyrosine kinase activity with a specific activity of about 20 nmol/min/mg.