Toward the molecular details of the nuclear pore complex.
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Amino Acid Sequence↗
Biomedical subjects
U Aebi
Publications and source records attributed to U Aebi.
Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin.
The human calcitonin (hCT) peptide hormone has a marked tendency to aggregate in aqueous solutions and to form long, thin fibrillar aggregates resulting in viscous and turbid dispersions. In this study, the in vitro aggregation products of hCT were systematically investigated using conventional transmission electron microscopy (CTEM) and in-lens field emission scanning electron microscopy. The mass per length of unstained/air-dried specimens was determined by scanning transmission electron microscopy. Irrespective of the sample preparation method and electron microscopic (EM) imaging mode employed, similar supramolecular assemblies were observed. Based on these EM data, it is proposed that hCT aggregation begins with the formation of approximately 4-nm-thick protofibrils. These protofibrils further interact via lateral association and coiling to form higher-order fibrillar assemblies, i.e., protofibril-ribbons, fibrils, fibril-ribbons, tubes, and multistranded cables. The concentration and history of the aggregated hCT solutions strongly influenced the relative frequency of the various hCT assemblies depicted. The supramolecular assemblies of hCT revealed distinct helical symmetries at their different levels of aggregation. A hypothetical mechanism assumed for aggregating solutions to form polymorphic fibrillar hCT assemblies is presented in a schematic model, and the supramolecular arrangement of hCT within the various polymorphic fibrillar aggregates is delineated.
Amino Acid Sequence↗
Real-time isocontouring and texture mapping meet new challenges in interactive molecular graphics applications.
A technique to extract solid isosurfaces from three-dimensional electron density data at high speed is presented. The ability to change the contouring threshold in real time renders the method a powerful tool for interactive analysis of proteins and their supramolecular assemblies, in order to compare and combine structural information gathered by different data acquisition methods. Chemical properties can effectively be mapped onto these isosurfaces by the use of texture mapping. The implications of these methods in combination with other visualization techniques are discussed, and a framework for their integration into a general-purpose molecular graphics toolkit is proposed.
Carbohydrate Conformation↗
Scanning tunneling and transmission electron microscopy on identical areas of biological specimens.
A methodology for tip and specimen-support manufacturing is described which allows for scanning tunneling microscopy (STM) and transmission electron microscopy (TEM) on identical areas of biological specimens, at comparable resolution. Topographs and dI/ds-maps were used to investigate tip-specimen interaction on native air-dried phage T4 polyheads where individual capsomeres and structural alterations upon repetitive scans have been observed at a tunnel current of 0.5 pA.
Microscopy, Electron, Scanning↗
The role of the head and tail domain in lamin structure and assembly: analysis of bacterially expressed chicken lamin A and truncated B2 lamins.
Nuclear lamins like cytoplasmic intermediate filament proteins exhibit a characteristic tripartite domain structure with a segmented alpha-helical rod domain flanked by an N-terminal head and a C-terminal tail domain. To examine the influence of the head and tail domains on the structure and assembly properties of nuclear lamins, we have engineered "headless," "tailless," and "rod" chicken lamin B2 cDNAs and expressed them in Escherichia coli. A full-length chicken lamin A cDNA was also expressed in E. coli, and the recombinant protein compared with the structure and assembly properties of full-length chicken lamin B2 (E. Heitlinger et al. (1991) J. Cell Biol. 113, 485-495). As with lamin B2, at their first level of structural organization, lamin A and the headless lamin B2 formed myosin-like dimers consisting of a 51- to 52-nm-long tail flanked by two globular heads at one end. Similarly, the tailless and rod lamin B2 fragments formed tropomyosin-like dimers consisting of a 51 to 52-nm-long rod. In contrast to the lateral mode of association of cytoplasmic IF dimers into four-chain tetramers, at their second level of structural organization, lamin A dimers, just as lamin B2 dimers (E. Heitlinger et al. (1991) J. Cell Biol. 113, 485-495), associated longitudinally to form polar head-to-tail polymers. Whereas dimers made of the truncated B2 headless and rod lamins had lost their propensity to associate head-to-tail, tailless lamin B2 dimers revealed an enhanced head-to-tail association. Finally, at their third level of structural organization, rather than assembling into stable 10-nm filaments, both lamin A and the three truncated B2 lamins formed paracrystalline arrays exhibiting distinct transverse banding patterns with axial repeats of either 24 or 48-49 nm depending on the species.
Animals↗
The nuclear lamina is a meshwork of intermediate-type filaments.
The nuclear lamina, a protein meshwork lining the nucleoplasmic surface of the inner nuclear membrane, is thought to provide a framework for organizing nuclear envelope structure and an anchoring site at the nuclear periphery for interphase chromatin. In several higher eukaryotic cells, the lamina appears to be a polymer comprised mainly of one to three immunologically related polypeptides of relative molecular mass (Mr) 60,000-75,000 (60-70K) termed lamins. Three lamins (A, B, and C) are typically present in mammalian somatic cells. Previous studies on nuclear envelopes of rat liver and Xenopus oocytes suggested that the lamina has a fibrillar or filamentous substructure. Interestingly, protein sequences recently deduced for human lamins A and C from complementary DNA clones indicate that both of these polypeptides contain a region of approximately 350 amino acids very similar in sequence to the coiled-coil alpha-helical rod domain that characterizes all intermediate-type filament (IF) proteins. Here we analyse the supramolecular organization of the native nuclear lamina and the structure and assembly properties of purified lamins, and show that the lamins constitute a previously unrecognized class of IF polypeptides.
Animals↗
Outcome of 100 randomly positioned children of very low birthweight at 2 years.
Prematurely born children often show a tendency to adopt extensor motor patterns during the first years of life. These children and especially those children of very low birthweight are considered to be at high risk for abnormal development. Positioning in an ordinary manner or in a more flexed position imposed at random during the neonatal period until discharge from hospital did not have a statistically significant influence on the development of these children at 24 months after term. Analysis of the optimality score of the 100 randomly selected children, born consecutively at the University Women's Hospital, Bern, showed a significant influence of prenatal optimality and congenital malformations on their later outcome.
Child Development↗