Effects of chemical functionalization on electronic transport in carbon nanobuds

Carbon nanobuds form a class of hybrid structures consisting of carbon nanotubes onto which fullerene types of units are covalently grown. Due to higher electrophilicity and curvature of the fullerene moiety a carbon nanobud exhibits higher reactivity compared to a plain nanotube. In this paper we study how the electronic structure and transport properties of carbon nanobuds are affected by chemical modification. The studied model systems comprise carbon nanobuds that are chemically modified by attaching Li and F atoms as well as tetrathiafulvalene molecules. We use the density functional theory combined with Landauer-Büttiker electron transport formalism. According to the simulations, the attached units change the relative positions of the Fermi levels, creating a distinctive effect on the electronic transport properties along associated carbon nanotubes. In semiconducting nanotubes the change in the conductance is systematic and should be detectable in experiments. Hence, the carbon nanobuds are potential candidates for sensor applications.Peer reviewe

Positive Selection for New Disease Mutations in the Human Germline: Evidence from the Heritable Cancer Syndrome Multiple Endocrine Neoplasia Type 2B

Multiple endocrine neoplasia type 2B (MEN2B) is a highly aggressive thyroid cancer syndrome. Since almost all sporadic cases are caused by the same nucleotide substitution in the RET proto-oncogene, the calculated disease incidence is 100–200 times greater than would be expected based on the genome average mutation frequency. In order to determine whether this increased incidence is due to an elevated mutation rate at this position (true mutation hot spot) or a selective advantage conferred on mutated spermatogonial stem cells, we studied the spatial distribution of the mutation in 14 human testes. In donors aged 36–68, mutations were clustered with small regions of each testis having mutation frequencies several orders of magnitude greater than the rest of the testis. In donors aged 19–23 mutations were almost non-existent, demonstrating that clusters in middle-aged donors grew during adulthood. Computational analysis showed that germline selection is the only plausible explanation. Testes of men aged 75–80 were heterogeneous with some like middle-aged and others like younger testes. Incorporating data on age-dependent death of spermatogonial stem cells explains the results from all age groups. Germline selection also explains MEN2B's male mutation bias and paternal age effect. Our discovery focuses attention on MEN2B as a model for understanding the genetic and biochemical basis of germline selection. Since RET function in mouse spermatogonial stem cells has been extensively studied, we are able to suggest that the MEN2B mutation provides a selective advantage by altering the PI3K/AKT and SFK signaling pathways. Mutations that are preferred in the germline but reduce the fitness of offspring increase the population's mutational load. Our approach is useful for studying other disease mutations with similar characteristics and could uncover additional germline selection pathways or identify true mutation hot spots

Stable Lithium Argon compounds under high pressure

High pressure can fundamentally alter the bonding patterns of chemical elements. Its effects include stimulating elements thought to be “inactive” to form unexpectedly stable compounds with unusual chemical and physical properties. Here, using an unbiased structure search method based on CALYPSO methodology and density functional total energy calculations, the phase stabilities and crystal structures of Li−Ar compounds are systematically investigated at high pressure up to 300 GPa. Two unexpected Li(m)Ar(n) compounds (LiAr and Li(3)Ar) are predicted to be stable above 112 GPa and 119 GPa, respectively. A detailed analysis of the electronic structure of LiAr and Li(3)Ar shows that Ar in these compounds attracts electrons and thus behaves as an oxidizing agent. This is markedly different from the hitherto established chemical reactivity of Ar. Moreover, we predict that the P4/mmm phase of Li(3)Ar has a superconducting transition temperature of 17.6 K at 120 GPa

Sorting of proteins to vacuoles in plant cells

for correspondence

Formation of Tetrahydrofurano-, Aryltetralin, and Butyrolactone Norlignans through the Epoxidation of 9-Norlignans

Epoxidation of the C=C double bond in unsaturated norlignans derived from hydroxymatairesinol was studied. The intermediate epoxides were formed in up to quantitative conversions and were readily further transformed into tetrahydrofuran, aryltetralin, and butyrolactone products—in diastereomeric mixtures—through ring-closing reactions and intramolecular couplings. For epoxidation, the classical Prilezhaev reaction, using stoichiometric amounts of meta-chloroperbenzoic acid (mCPBA), was used. As an alternative method, a catalytic system using dimeric molybdenum-complexes [MoO2L]2 with ONO- or ONS-tridentate Schiff base ligands and aqueous tert-butyl hydroperoxide (TBHP) as oxidant was used on the same substrates. Although the epoxidation was quantitative when using the Mo-catalysts, the higher temperatures led to more side-products and lower yields. Kinetic studies were also performed on the Mo-catalyzed reactions

Oxidative Transformations of Lignans

Numerous oxidative transformations of lignan structures have been reported in the literature. In this paper we present an overview on the current findings in the field. The focus is put on transformations targeting a specific structure, a specific reaction, or an interconversion of the lignan skeleton. Oxidative transformations related to biosynthesis, antioxidant measurements, and total syntheses are mostly excluded. Non-metal mediated as well as metal mediated oxidations are reported, and mechanisms based on hydrogen abstractions, epoxidations, hydroxylations, and radical reactions are discussed for the transformation and interconversion of lignan structures. Enzymatic oxidations, photooxidation, and electrochemical oxidations are also briefly reported

A Study of the Interactions in a Extended Unsupported Gold-Silver Chain.

The complex [Ag(Py)3][Au(C6F5)2]·Py (1) (Py = pyridine) has been prepared by the reaction of NBu4[Au(C6F5)2] with AgClO4 in the presence of pyridine. The crystallographic measurements indicate the presence of an extended unsupported one-dimensional chain of alternating gold and silver atoms. This arrangement is due to the formation of molecular Au-Ag ion pairs, to the -stacking of C6F5 and pyridine arene ligands and to the packing effects that lead to molecular ion pairs at short distance. Theoretical calculations based on approximate experimental distances and angles reveal the presence of both metallophilic Au1-Ag1 and aromatic C6F5-pyridine interactions. From a theoretical point of view the nature of the intermetallic attraction arises from both an ionic contribution and from dispersion-type correlation effects; the aromatic interaction is mainly due to dispersion-type correlation effects

The Glycosylation of the Aspartic Proteinases from Barley (Hordeum Vulgare L.) and Cardoon (Cynara Cardunculus L.)

Plant aspartic proteinases characterised at the molecular level contain one or more consensus N-glycosylation sites [Runeberg-Roos, P., Törmäkangas, K. & Östman, A. (1991) Eur. J. Biochem. 202, 102120131027; Asakura, T., Watanabe, H., Abe, K. & Arai, S. (1995) Eur. J. Biochem. 232, 77201383; Veríssimo, P., Faro, C., Moir, A. J. G., Lin, Y., Tang, J. & Pires, E. (1996) Eur. J. Biochem. 235, 76220137681. We found that the glycosylation sites are occupied for the barley (Hordeum vulgare L.) aspartic proteinase (Asn333) and the cardoon (Cynara cardunculus L.) aspartic proteinase, cardosin A (Asn70 and Asn363). The oligosaccharides from each site were released from peptide pools by enzymatic hydrolysis with peptide-N-glycanase A or by hydrazinolysis and their structures were determined by exoglycosidase sequencing combined with matrix-assisted laser desorption/ionization time of flight mass spectrometry. It was observed that 6% of the oligosaccharides from the first glycosylation site of cardosin A are of the oligomannose type. Modified type glycans with proximal Fuc and without Xyl account for about 82%, 14% and 3% of the total oligosaccharides from the first and the second glycosylation sites of cardosin A and from H. vulgare aspartic proteinase, respectively. Oligosaccharides with Xyl but without proximal Fuc were only detected in the latter proteinase (4%). Glycans with proximal Fuc and Xyl account for 6%, 86% and 92% of the total oligosaccharides from the first and second glycosylation sites of cardosin A and from H. vulgure aspartic proteinase, respectively