Development of a propulsion system for a biomimetic thruster

We studied theoretically and experimentally a biomimetic propulsion system inspired by the motility mechanisms of bacteria such as E. coli. Our goal was to investigate the effect of the ??complex?? filament of Rhizobium Meliloti bacteria on thrust force. The complex filament is a helically perturbed filament, similar to a plain filament threaded through a small helix. The propulsive performance of this system was estimated by modeling the dynamics of helical wave motion in viscous fluid. The model consists of a helical filament which is axially rotated at angular velocity ??. Resistive force theory (RFT) was applied to this model to calculate the thrust force and required torque. The Buckingham PI theorem (non-dimensional analysis) was also used to analyze the theoretical results. The procedure for making a complex filament with various pitch angles ?? _s from a small helix and plain filament is explained in detail. To validate the theoretical results for helical wave propulsion and compare the characteristics of complex and plain filaments together, an experiment was performed to measure the thrust forces in silicone oil. The experimental results agreed with the theoretical values predicted by RFT. The thrust forces of complex filaments depended on the shape of small helix winding. The maximum thrust force was achieved at a small helix pitch angle of ?? _s = 45°. In addition, we found that the thrust force generated by a complex filament had a value about 10% higher than that of a plain filament with the same equivalent diameter d _e .     

Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling

The bacterial flagellar filament is a helical propeller constructed from 11 protofilaments of a single protein, flagellin. The filament switches between left- and right-handed supercoiled forms when bacteria switch their swimming mode between running and tumbling. Supercoiling is produced by two different packing interactions of flagellin called L and R. In switching from L to R, the intersubunit distance ( approximately 52 A) along the protofilament decreases by 0.8 A. Changes in the number of L and R protofilaments govern supercoiling of the filament. Here we report the 2.0 A resolution crystal structure of a Salmonella flagellin fragment of relative molecular mass 41,300. The crystal contains pairs of antiparallel straight protofilaments with the R-type repeat. By simulated extension of the protofilament model, we have identified possible switch regions responsible for the bi-stable mechanical switch that generates the 0.8 A difference in repeat distance.     

柔性LED灯丝的发展进程与展望

柔性LED灯丝是一种新型的LED光源,将多颗倒装芯片串联封装在柔性透明基板制备成可任意弯曲与拉伸的灯丝,实现360°全角度发光。解决了刚性LED灯丝吸光、可塑性差、结构复杂、制造繁琐等问题,使LED灯丝得到进一步的应用与推广,推动了LED灯丝灯的发展。综述了柔性LED灯丝在封装结构、封装材料、封装工艺、散热技术等方面研究状况,对实际研究和应用有一定的指导意义。     

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.     

包囊游仆虫细胞的类中间纤维细胞骨架体系

应用生化分级抽提,并结合DGD包埋 去包埋透射电镜样品制备方法显示,包囊游仆虫营养细胞和休眠细胞中,均存在由直径10 nm左右的单根纤维及单根纤维聚集成的纤维束为结构单元形成的类中间纤维细胞骨架体系.其中,营养细胞的类中间纤维构成的细胞质三维网架,在细胞膜内缘以较密集的纤维网占有了整个表质层,在表质层内缘的细胞质深部纤维形成较松散的网络,网内常见附着有细胞器及一些电子密度颗粒;核纤层位于大核核膜内缘,纤维紧密聚集成网;核骨架纤维网分布比较致密,未见有电子密度颗粒附着.休眠细胞中含有与营养细胞相似的纤维网架结构,但位于细胞内不同层次的纤维网比营养细胞中的同种结构要致密得多,这可能与纤毛虫形成包囊时细胞大范围的收缩有关.并且值得注意的是,在休眠细胞包囊壁的内层壁中也观察到相似于中间纤维的纤维网络,其纤维网均匀和致密地分布在整个包囊壁层中.电泳图谱显示,纤毛虫形成包囊后,保留了营养细胞中的部分蛋白条带,失去了部分条带,新产生了一些特异的条带.结果表明,包囊游仆虫的类中间纤维 核骨架体系,是细胞在营养条件下和休眠状态下都稳定存在的结构,它可能起到比微管类骨架更重要的作用.并且休眠细胞中该体系产生的一些特异蛋白条带,可能是纤毛虫休眠生命活动中的重要蛋白.     

Kinematics and forces of a flexible body in Karman vortex street

Experiments of a flexible filament in the wake of a cylinder and in free stream were conducted in a vertical soap film tunnel. The experiments distinctly visualized the movement of the filament. Based on the experimental kinematic results, a 2-d panel method was used to calculate the forces acting on the filament. The experiment and numerical results revealed that different from that in free stream, the filament in Karman vortex street flapped at the same frequency as the vortex street, and with smaller amplitude and larger curvature. The filament suffered an evident thrust in Karman vortex street, while a drag appeared in the case of free stream. The dependence of the drag coefficient on the phase relation between the movement of the filament and the Karman vortex street was also studied. Supported by the National Natural Science Foundation of China (Grant No. 10832010) and Innovation Project of Chinese Academy of Sciences (Grant No. KJCX2-YW-L05)     

Flexible filaments in a flowing soap film as a model for one-dimensional flags in a two-dimensional wind

The dynamics of swimming fish and flapping flags involves a complicated interaction of their deformable shapes with the surrounding fluid flow. Even in the passive case of a flag, the flag exerts forces on the fluid through its own inertia and elastic responses, and is likewise acted on by hydrodynamic pressure and drag. But such couplings are not well understood. Here we study these interactions experimentally, using an analogous system of flexible filaments in flowing soap films. We find that, for a single filament (or 'flag') held at its upstream end and otherwise unconstrained, there are two distinct, stable dynamical states. The first is a stretched-straight state: the filament is immobile and aligned in the flow direction. The existence of this state seems to refute the common belief that a flag is always unstable and will flap. The second is a flapping state: the filament executes a sinuous motion in a manner akin to the flapping of a flag in the wind. We study further the hydrodynamically coupled interaction between two such filaments, and demonstrate the existence of four different dynamical states.     

Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins

Most nucleated cells crawl about by extending a pseudopod that is driven by the polymerization of actin filaments in the cytoplasm behind the leading edge of the plasma membrane. These actin filaments are linked into a network by Y-branches, with the pointed end of each filament attached to the side of another filament and the rapidly growing barbed end facing forward. Because Arp2/3 complex nucleates actin polymerization and links the pointed end to the side of another filament in vitro, a dendritic nucleation model has been proposed in which Arp2/3 complex initiates filaments from the sides of older filaments. Here we report, by using a light microscopy assay, many new features of the mechanism. Branching occurs during, rather than after, nucleation by Arp2/3 complex activated by the Wiskott-Aldrich syndrome protein (WASP) or Scar protein; capping protein and profilin act synergistically with Arp2/3 complex to favour branched nucleation; phosphate release from aged actin filaments favours dissociation of Arp2/3 complex from the pointed ends of filaments; and branches created by Arp2/3 complex are relatively rigid. These properties result in the automatic assembly of the branched actin network after activation by proteins of the WASP/Scar family and favour the selective disassembly of proximal regions of the network.     

Insights into DNA recombination from the structure of a RAD51-BRCA2 complex

The breast cancer susceptibility protein BRCA2 controls the function of RAD51, a recombinase enzyme, in pathways for DNA repair by homologous recombination. We report here the structure of a complex between an evolutionarily conserved sequence in BRCA2 (the BRC repeat) and the RecA-homology domain of RAD51. The BRC repeat mimics a motif in RAD51 that serves as an interface for oligomerization between individual RAD51 monomers, thus enabling BRCA2 to control the assembly of the RAD51 nucleoprotein filament, which is essential for strand-pairing reactions during DNA recombination. The RAD51 oligomerization motif is highly conserved among RecA-like recombinases, highlighting a common evolutionary origin for the mechanism of nucleoprotein filament formation, mirrored in the BRC repeat. Cancer-associated mutations that affect the BRC repeat disrupt its predicted interaction with RAD51, yielding structural insight into mechanisms for cancer susceptibility.     

Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain

The conserved formin homology 2 (FH2) domain nucleates actin filaments and remains bound to the barbed end of the growing filament. Here we report the crystal structure of the yeast Bni1p FH2 domain in complex with tetramethylrhodamine-actin. Each of the two structural units in the FH2 dimer binds two actins in an orientation similar to that in an actin filament, suggesting that this structure could function as a filament nucleus. Biochemical properties of heterodimeric FH2 mutants suggest that the wild-type protein equilibrates between two bound states at the barbed end: one permitting monomer binding and the other permitting monomer dissociation. Interconversion between these states allows processive barbed-end polymerization and depolymerization in the presence of bound FH2 domain. Kinetic and/or thermodynamic differences in the conformational and binding equilibria can explain the variable activity of different FH2 domains as well as the effects of the actin-binding protein profilin on FH2 function.     

A model for SOS-lesion-targeted mutations in Escherichia coli

The UmuD'2C protein complex (Escherichia coli pol V) is a low-fidelity DNA polymerase (pol) that copies damaged DNA in the presence of RecA, single-stranded-DNA binding protein (SSB) and the beta,gamma-processivity complex of E. coli pol III (ref. 4). Here we propose a model to explain SOS-lesion-targeted mutagenesis, assigning specific biochemical functions for each protein during translesion synthesis. (SOS lesion-targeted mutagenesis occurs when pol V is induced as part of the SOS response to DNA damage and incorrectly incorporates nucleotides opposite template lesions.) Pol V plus SSB catalyses RecA filament disassembly in the 3' to 5' direction on the template, ahead of the polymerase, in a reaction that does not involve ATP hydrolysis. Concurrent ATP-hydrolysis-driven filament disassembly in the 5' to 3' direction results in a bidirectional stripping of RecA from the template strand. The bidirectional collapse of the RecA filament restricts DNA synthesis by pol V to template sites that are proximal to the lesion, thereby minimizing the occurrence of untargeted mutations at undamaged template sites.     

Single-molecule imaging of DNA pairing by RecA reveals a three-dimensional homology search

DNA breaks can be repaired with high fidelity by homologous recombination. A ubiquitous protein that is essential for this DNA template-directed repair is RecA. After resection of broken DNA to produce single-stranded DNA (ssDNA), RecA assembles on this ssDNA into a filament with the unique capacity to search and find DNA sequences in double-stranded DNA (dsDNA) that are homologous to the ssDNA. This homology search is vital to recombinational DNA repair, and results in homologous pairing and exchange of DNA strands. Homologous pairing involves DNA sequence-specific target location by the RecA-ssDNA complex. Despite decades of study, the mechanism of this enigmatic search process remains unknown. RecA is a DNA-dependent ATPase, but ATP hydrolysis is not required for DNA pairing and strand exchange, eliminating active search processes. Using dual optical trapping to manipulate DNA, and single-molecule fluorescence microscopy to image DNA pairing, we demonstrate that both the three-dimensional conformational state of the dsDNA target and the length of the homologous RecA-ssDNA filament have important roles in the homology search. We discovered that as the end-to-end distance of the target dsDNA molecule is increased, constraining the available three-dimensional (3D) conformations of the molecule, the rate of homologous pairing decreases. Conversely, when the length of the ssDNA in the nucleoprotein filament is increased, homology is found faster. We propose a model for the DNA homology search process termed 'intersegmental contact sampling', in which the intrinsic multivalent nature of the RecA nucleoprotein filament is used to search DNA sequence space within 3D domains of DNA, exploiting multiple weak contacts to rapidly search for homology. Our findings highlight the importance of the 3D conformational dynamics of DNA, reveal a previously unknown facet of the homology search, and provide insight into the mechanism of DNA target location by this member of a universal family of proteins.     

异收缩长丝仿毛原料及其织物风格研究

以高收缩丝、微细旦POY丝、低弹丝(DTY)等差别化长丝为原料,加工成异收缩复合空变纱,对其纱线及仿毛织物进行了基本力学性能研究,对比纯毛织物得出:高收缩涤纶丝(单丝纤度为0.3tex左右)与POY皮芯复合空变加工成异收缩变形纱,其织物仿毛效果好;涤纶混色空变纱织物或与网络弹力丝进行交织的织物仿毛效果也较好。     

Site-specific phosphorylation induces disassembly of vimentin filaments in vitro

Intermediate filaments are a major component of the cytoskeleton of eukaryotic cells. Although there appear to be at least five distinct classes of these filaments, cells of mesenchymal origin and most cells in culture contain the intermediate filament composed of the subunit protein vimentin. Vimentin exists in a nonphosphorylated as well as in a phosphorylated form, and there is increased phosphorylation of this protein when the filament undergoes marked redistribution in various cells. The role of phosphorylation on assembly-disassembly and organization of the vimentin filament has remained obscure. We report here a stable and purified system allowing biochemical examination of vimentin filament assembly and disassembly. Using this in vitro system, we carried out stoichiometrical phosphorylations, using purified protein kinases. We obtained evidence for site-specific, phosphorylation-dependent disassembly of the vimentin filament.     

海水水族箱系统微生物生态平衡的初步研究

本研究将ＰＦＵ引入水族箱生态系中定量采集附生的硝化细菌，荧光显微计数法直接计数水族箱中具有代谢活性的细菌数量的变化．研究了新建海水水族箱系统中硝化细菌的成熟过程．结果表明：在新建海水水族箱系统中细菌生态平衡的初步达成约需４０ｄ，验证了其他学者通过水质分析评价细菌功能的结论．应用ＰＦＵ定量采集附生在滤床上的硝化细菌．及ＡＯＤＣ和ＤＶＣ法直接测定水体中具有代谢活性的细菌数量为研究细菌的数量动态提供了一种简便、快速而又准确的方法和手段     

Synthetic biology: engineering Escherichia coli to see light

We have designed a bacterial system that is switched between different states by red light. The system consists of a synthetic sensor kinase that allows a lawn of bacteria to function as a biological film, such that the projection of a pattern of light on to the bacteria produces a high-definition (about 100 megapixels per square inch), two-dimensional chemical image. This spatial control of bacterial gene expression could be used to 'print' complex biological materials, for example, and to investigate signalling pathways through precise spatial and temporal control of their phosphorylation steps.     

缠绕圆筒的组合变形及在扭振控制中的应用

分析了纤维增强复合材料缠绕圆筒的组合变形和力学性质,提出了一种采用纤维缠绕复合材料技术消减特定激振条件下振幅的方法,应用于轴类零件扭转振动的控制,得到了各向异性缠绕套筒的减振设计公式,     

Structural insight into filament formation by mammalian septins

Septins are GTP-binding proteins that assemble into homo- and hetero-oligomers and filaments. Although they have key roles in various cellular processes, little is known concerning the structure of septin subunits or the organization and polarity of septin complexes. Here we present the structures of the human SEPT2 G domain and the heterotrimeric human SEPT2-SEPT6-SEPT7 complex. The structures reveal a universal bipolar polymer building block, composed of an extended G domain, which forms oligomers and filaments by conserved interactions between adjacent nucleotide-binding sites and/or the amino- and carboxy-terminal extensions. Unexpectedly, X-ray crystallography and electron microscopy showed that the predicted coiled coils are not involved in or required for complex and/or filament formation. The asymmetrical heterotrimers associate head-to-head to form a hexameric unit that is nonpolarized along the filament axis but is rotationally asymmetrical. The architecture of septin filaments differs fundamentally from that of other cytoskeletal structures.     

天然家蚕抗菌肽对人白细胞及巨噬细胞淋巴瘤细胞骨架系统作用的比较

报道了天然家蚕抗菌肽ＣＭ４对离体Ｕ９３７癌细胞骨架及核骨架损伤作用的扫描电镜观察。随着时间的延长，经天然家蚕抗菌肽ＣＭ４作用后的癌细胞骨架断裂，固缩成团状；癌细胞核骨架断裂，部分凝聚成团，结构不完整。相同剂量的天然家蚕抗菌肽ＣＭ４与正常人白细胞作用后细胞骨架及核骨架未见损伤现象。说明天然抗菌肽与重组抗菌肽的抗癌作用相同。     

Palindromic assembly of the giant muscle protein titin in the sarcomeric Z-disk

The Z-disk of striated and cardiac muscle sarcomeres is one of the most densely packed cellular structures in eukaryotic cells. It provides the architectural framework for assembling and anchoring the largest known muscle filament systems by an extensive network of protein-protein interactions, requiring an extraordinary level of mechanical stability. Here we show, using X-ray crystallography, how the amino terminus of the longest filament component, the giant muscle protein titin, is assembled into an antiparallel (2:1) sandwich complex by the Z-disk ligand telethonin. The pseudosymmetric structure of telethonin mediates a unique palindromic arrangement of two titin filaments, a type of molecular assembly previously found only in protein-DNA complexes. We have confirmed its unique architecture in vivo by protein complementation assays, and in vitro by experiments using fluorescence resonance energy transfer. The model proposed may provide a molecular paradigm of how major sarcomeric filaments are crosslinked, anchored and aligned within complex cytoskeletal networks.