A system of DNA "tiles" that is designed to assemble to form two-dimensional arrays is observed to form narrow ribbons several micrometers in length. The uniform width of the ribbons and lack of frayed edges lead us to propose that they are arrays that have curled and closed on themselves to form tubes. This proposal is confirmed by the observation of tubes with helical order.

Weaving with DNA: A DNA‐binding protein was used to control the structure of a self‐assembled 2D crystal. In the absence of protein, four oligonucleotides hybridize to form a Kagome lattice of interwoven double helices with p3 symmetry (see image). Addition of protein RuvA during assembly changes the symmetry and connectivity to give a DNA–protein crystal with an approximately square unit cell.

We present a facile method for linking recombinant proteins to DNA. It is based on the nickel-mediated interaction between a hexahistidine tag (His(6)-tag) and DNA functionalized with three nitrilotriacetic acid (NTA) groups. The resulting DNA-protein linkage is site-specific. It can be broken quickly and controllably by the addition of a chelating agent that binds nickel. We have used this new linker to bind proteins to a variety of DNA motifs commonly used in the fabrication of nanostructures by DNA self-assembly.

Weben mit DNA: Mit einem DNA‐bindenden Protein lässt sich die Struktur eines selbstorganisierten 2D‐Kristalls steuern. Ohne das Protein hybridisieren vier Oligonucleotide zu miteinander verwobenen Doppelhelices mit p3‐Symmetrie (siehe Bild). Zugabe des Proteins RuvA während der Selbstorganisation ändert die Symmetrie und Verknüpfung, und es resultiert ein DNA‐Protein‐Kristall mit annähernd quadratischer Elementarzelle.

The interactions between phospholipid molecules in suspensions have been studied by using mass spectrometry. Electrospray mass spectra of homogeneous preparations formed from three different phospholipid molecules demonstrate that under certain conditions interactions between 90 and 100 lipid molecules can be preserved. In the presence of apolipoprotein C-II, a phospholipid binding protein, a series of lipid molecules and the protein were observed in complexes. The specificity of binding was demonstrated by proteolysis; the resulting mass spectra reveal lipid-bound peptides that encompass the proposed lipid-binding domain. The mass spectra of heterogeneous suspensions and their complexes with apolipoprotein C-II demonstrate that the protein binds simultaneously to two different phospholipids. Moreover, when apolipoprotein C-II is added to lipid suspensions formed with local concentrations of the same lipid molecule, the protein is capable of remodeling the distribution to form one that is closer to a statistical arrangement. These observations demonstrate a capacity for apolipoprotein C-II to change the topology of the phospholipid surface. More generally, these results highlight the fact that mass spectrometry can be used to probe lipid interactions in both homogeneous and heterogeneous suspensions and demonstrate reorganization of the distribution of lipids upon surface binding of apolipoprotein C-II.

We describe the three-layer logpile (3LL), a two-dimensional DNA array which self-assembles from four synthetic oligonucleotides via a four-armed Holliday junction motif. It consists of three layers of helices, each running at 60 degrees to the others. DNA arrays can be used as periodic templates to create, for example, synthetic protein crystals: this array is designed to maximize structural order by ensuring that helices run continuously, without bending, through the structure. UV absorbance measurements show a rate-dependent hysteresis associated with the assembly of the 3LL. Negative-stain transmission electron microscopy (TEM) of 3LL samples shows that the arrays form extensive sheets (approximately microm(2)) and a process of iterative correlation mapping and averaging of small subsets of digitized TEM micrographs yields an averaged projection image that is consistent with a computer-generated model of the crystal.

Proprotein convertase subtilisin kexin 9 (PCSK9) is a serine protease with a key role in regulating plasma low-density lipoprotein (LDL) concentration. Since its discovery via parallel molecular biology and clinical genetics studies in 2003, work to characterize PCSK9 has shed new light on the life-cycle of the low-density lipoprotein receptor and the molecular basis of familial hypercholesterolaemia. These discoveries have also led to the advent of the PCSK9 inhibitors, a new generation of low-density lipoprotein cholesterol (LDL-C) lowering drugs. Clinical trials have shown these agents to be both safe and capable of unprecedented reductions in LDL-C, and it is hoped they may herald a new era of cardiovascular disease prevention. As such, the still evolving PCSK9 story serves as a particularly successful example of translational medicine. This review provides a summary of the principal PCSK9 research findings, which underpin our current understanding of its function and clinical relevance.