In situ backscattered electron imaging study of the effect of annealing on the deformation behaviors of Ni electroformed from additive-free and saccharin-containing sulfamate solutions

The Ni samples were electroformed from additive-free(AF) and saccharin-containing(SC) sulfamate solutions, respectively. In situ backscattered electron(BSE) imaging, electron backscatter diffraction(EBSD), and electron-probe microanalysis(EPMA) were used to investigate the effect of annealing on the deformation behaviors of the AF and SC samples. The results indicate that columnar grains of the as-deposited AF sample had an approximated average width of 3 μm and an approximated aspect ratio of 8. The average width of columnar grains of the as-deposited SC sample was reduced to approximately 400 nm by the addition of saccharin to the electrolyte. A few very-large grains distributed in the matrix of the SC sample after annealing. No direct evidence indicated that S segregated at the grain boundaries before or after annealing. The average value of the total elongations of the SC samples decreased from 16% to 6% after annealing, whereas that of the AF samples increased from 18% to 50%. The dislocation recovery in grain-boundary areas of the annealed AF sample was reduced, which contributed to the appearance of microvoids at the triple junctions. The incompatibility deformation between very-large grains and fine grains contributed to the brittle fracture behavior of the annealed SC Ni.     

金纳米薄膜面向导热系数的实验研究

基于电子束物理气相沉积法制备纳米薄膜的悬浮工艺，采用一维稳态恒热流加热法实验测量了80—300K厚度为23nm金薄膜的面向导热系数．研究表明金纳米薄膜的面向导热系数有非常显著的尺寸效应：金纳米薄膜的面向导热系数大大低于体材料的值，并且导热系数随温度的升高而增大，这一趋势与体材料导热系数的温度依赖性相反；同时，金纳米薄膜的Lorenz数大约为体材料值的3倍，并且随着温度的升高有减小的趋势，表明Wiedemann-Franz定律对于金纳米薄膜不再适用．     

Sliding movement of single actin filaments on one-headed myosin filaments

The myosin molecule consists of two heads, each of which contains an enzymatic active site and an actin-binding site. The fundamental problem of whether the two heads function independently or cooperatively during muscle contraction has been studied by methods using an actomyosin thread, superprecipitation and chemical modification of muscle fibres. No clear conclusion has yet been reached. We have approached this question using an assay system in which sliding movements of fluorescently labelled single actin filaments along myosin filaments can be observed directly. Here, we report direct measurement of the sliding of single actin filaments along one-headed myosin filaments in which the density of heads was varied over a wide range. Our results show that cooperative interaction between the two heads of myosin is not essential for inducing the sliding movement of actin filaments.     

Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist

The parasympathetic branch of the autonomic nervous system regulates the activity of multiple organ systems. Muscarinic receptors are G-protein-coupled receptors that mediate the response to acetylcholine released from parasympathetic nerves. Their role in the unconscious regulation of organ and central nervous system function makes them potential therapeutic targets for a broad spectrum of diseases. The M2 muscarinic acetylcholine receptor (M2 receptor) is essential for the physiological control of cardiovascular function through activation of G-protein-coupled inwardly rectifying potassium channels, and is of particular interest because of its extensive pharmacological characterization with both orthosteric and allosteric ligands. Here we report the structure of the antagonist-bound human M2 receptor, the first human acetylcholine receptor to be characterized structurally, to our knowledge. The antagonist 3-quinuclidinyl-benzilate binds in the middle of a long aqueous channel extending approximately two-thirds through the membrane. The orthosteric binding pocket is formed by amino acids that are identical in all five muscarinic receptor subtypes, and shares structural homology with other functionally unrelated acetylcholine binding proteins from different species. A layer of tyrosine residues forms an aromatic cap restricting dissociation of the bound ligand. A binding site for allosteric ligands has been mapped to residues at the entrance to the binding pocket near this aromatic cap. The structure of the M2 receptor provides insights into the challenges of developing subtype-selective ligands for muscarinic receptors and their propensity for allosteric regulation.     

Haploinsufficiency of NSD1 causes Sotos syndrome

We isolated NSD1 from the 5q35 breakpoint in an individual with Sotos syndrome harboring a chromosomal translocation. We identified 1 nonsense, 3 frameshift and 20 submicroscopic deletion mutations of NSD1 among 42 individuals with sporadic cases of Sotos syndrome. The results indicate that haploinsufficiency of NSD1 is the major cause of Sotos syndrome.     

Force measurements by micromanipulation of a single actin filament by glass needles

Single actin filaments (approximately 7 nm in diameter) labelled with fluorescent phalloidin can be clearly seen by video-fluorescence microscopy. This technique has been used to observe motions of single filaments in solution and in several in vitro movement assays. In a further development of the technique, we report here a method to catch and manipulate a single actin filament (F-actin) by glass microneedles under conditions in which external force on the filament can be applied and measured. Using this method, we directly measured the tensile strength of a filament (the force necessary to break the bond between two actin monomers) and the force required for a filament to be moved by myosin or its proteolytic fragment bound to a glass surface in the presence of ATP. The first result shows that the tensile strength of the F-actin-phalloidin complex is comparable with the average force exerted on a single thin filament in muscle fibres during isometric contraction. This force is increased only slightly by tropomyosin. The second measurement shows that the myosin head (subfragment-1) can produce the same ATP-dependent force as intact myosin. The magnitude of this force is comparable with that produced by each head of myosin in muscle during isometric contraction.