Windmilling of the rotor of a turbojet engine with an axial-flow compressor under flight conditions

The concept of rotor windmilling is understood to mean rotation of the rotor caused solely by the energy of the air (not gas) streaming through the apertures between the blades (under conditions of power shut-off) under the action of dynamic pressure. The concept of windmilling is analyzed for an engine with an axial-flow compressor, showing that windmilling must be taken into account in such cases as in-flight reignition of the engine. A graph-analytic method for determining the range of windmilling is proposed

Odsumporavanje čelika i sirovog željeza

Metallurgical slag qualities must be defined by the whole complex of physico - chemical characteristics, such as an oxidative ability, optical basicity, sulphide capacity up to slag fluidity, its surface tension etc. The understanding of regulation of basic physico - chemical qualities of molten metals and slag depending on a chemical structure and a temperature has its importance at the level of the metallurgical process control. Presented paper deals with the possibilities how to exploit the sulphidic capacity for the desulphurisation evaluation in course of the metal reafining in the oxygen converter based on the set of the operational data. The integral part of the work is the process of the pig iron desulphurisation.Kakvoća metalurške troske je definirana kompleksom fizikalno-kemijskih karakteristika, kao što su oksidacijska sposobnost, optimalna bazičnost, sulfidni kapacitet, ali i tečljivost troske, površinska napetost itd. Poznavanje mogućnosti regulacije temeljnih fizikalno-kemijskih kakvoć a tekućeg metala i troske ovisno o kemijskom sastavu i temperaturi osiguravaju vođenje metalurških procesa. U članku se daju mogućnosti kako rabiti sulfidni kapacitet za vrednovanje odsumporavanja tijekom rafinacije u kiskovom konvertoru pri danim pokazateljima. Članak je dopunjen i odsumporavanjem sirovog željeza

Vinculin Motion Modes Analysis with Elastic Network Model

Vinculin is an important protein for the linkage between adhesion molecules and the actin cytoskeleton. The activation mechanism of vinculin is still controversial. In order to provide useful information for a better understanding of its activation, we analyze the motion mode of vinculin with elastic network model in this work. The results show that, to some extent, the five domains will present structural rigidity in the motion process. The differences between the structure fluctuations of these domains are significant. When vinculin interacted with other partners, the central long alpha-helix of the first domain becomes bent. This bending deformation can weaken the interaction between the first domain and the tail domain. This motion mode of the first domain is in good agreement with the information extracted from some realistic complex structures. With the aid of the anisotropy elastic network mode, we analyze the motion directions of these domains. The fourth domain has a rotational motion. This rotation is favorable for the releasing of the tail domain from the pincer-like clamp, which is formed by the first and the third domain. All these motion modes are an inherent feature of the structure, and these modes mainly depend on the topology character of the structure

A Helix Replacement Mechanism Directs Metavinculin Functions

Cells require distinct adhesion complexes to form contacts with their neighbors or the extracellular matrix, and vinculin links these complexes to the actin cytoskeleton. Metavinculin, an isoform of vinculin that harbors a unique 68-residue insert in its tail domain, has distinct actin bundling and oligomerization properties and plays essential roles in muscle development and homeostasis. Moreover, patients with sporadic or familial mutations in the metavinculin-specific insert invariably develop fatal cardiomyopathies. Here we report the high resolution crystal structure of the metavinculin tail domain, as well as the crystal structures of full-length human native metavinculin (1,134 residues) and of the full-length cardiomyopathy-associated ΔLeu954 metavinculin deletion mutant. These structures reveal that an α-helix (H1′) and extended coil of the metavinculin insert replace α-helix H1 and its preceding extended coil found in the N-terminal region of the vinculin tail domain to form a new five-helix bundle tail domain. Further, biochemical analyses demonstrate that this helix replacement directs the distinct actin bundling and oligomerization properties of metavinculin. Finally, the cardiomyopathy associated ΔLeu954 and Arg975Trp metavinculin mutants reside on the replaced extended coil and the H1′ α-helix, respectively. Thus, a helix replacement mechanism directs metavinculin's unique functions

Adhesions Assemble!—Autoinhibition as a Major Regulatory Mechanism of Integrin-Mediated Adhesion

The advent of cell-cell and cell-extracellular adhesion enabled cells to interact in a coherent manner, forming larger structures and giving rise to the development of tissues, organs and complex multicellular life forms. The development of such organisms required tight regulation of dynamic adhesive structures by signaling pathways that coordinate cell attachment. Integrin-mediated adhesion to the extracellular matrix provides cells with support, survival signals and context-dependent cues that enable cells to run different cellular programs. One mysterious aspect of the process is how hundreds of proteins assemble seemingly spontaneously onto the activated integrin. An emerging concept is that adhesion assembly is regulated by autoinhibition of key proteins, a highly dynamic event that is modulated by a variety of signaling events. By enabling precise control of the activation state of proteins, autoinhibition enables localization of inactive proteins and the formation of pre-complexes. In response to the correct signals, these proteins become active and interact with other proteins, ultimately leading to development of cell-matrix junctions. Autoinhibition of key components of such adhesion complexes—including core components integrin, talin, vinculin, and FAK and important peripheral regulators such as RIAM, Src, and DLC1—leads to a view that the majority of proteins involved in complex assembly might be regulated by intramolecular interactions. Autoinhibition is relieved via multiple different signals including post-translation modification and proteolysis. More recently, mechanical forces have been shown to stabilize and increase the lifetimes of active conformations, identifying autoinhibition as a means of encoding mechanosensitivity. The complexity and scope for nuanced adhesion dynamics facilitated via autoinhibition provides numerous points of regulation. In this review, we discuss what is known about this mode of regulation and how it leads to rapid and tightly controlled assembly and disassembly of cell-matrix adhesion

Structural and biophysical properties of the integrin-associated cytoskeletal protein talin

Talin is a large cytoskeletal protein (2541 amino acid residues) which plays a key role in integrin-mediated events that are crucial for cell adhesion, migration, proliferation and survival. This review summarises recent work on the structure of talin and on some of the structurally better defined interactions with other proteins. The N-terminal talin head (approx. 50 kDa) consists of an atypical FERM domain linked to a long flexible rod (approx. 220 kDa) made up of a series of amphipathic helical bundle domains. The F3 FERM subdomain in the head binds the cytoplasmic tail of integrins, but this interaction can be inhibited by an interaction of F3 with a helical bundle in the talin rod, the so-called “autoinhibited form” of the molecule. The talin rod contains a second integrin-binding site, at least two actin-binding sites and a large number of binding sites for vinculin, which is important in reinforcing the initial integrin–actin link mediated by talin. The vinculin binding sites are defined by hydrophobic residues buried within helical bundles, and these must unfold to allow vinculin binding. Recent experiments suggest that this unfolding may be mediated by mechanical force exerted on the talin molecule by actomyosin contraction

Undergraduate Teaching and Research Experience through Peer Instruction and Laboratory Occupational Training (PILOT)

Students gain many benefits from their participation in undergraduate research. Unfortunately, the one student one mentor paradigm Friday, October 8th, Abstracts 6 | www.researchsymposium.ucf.edu www.researchsymposium.ucf.edu | 7 is limited to a few select students. The Burnett School of Biomedical Sciences at UCF educates 2,300 undergraduates majoring in either Biotechnology or Molecular Biology and Microbiology. About 90 students work on research projects in BSBS faculty labs. This is a substantial number, but it only represents 4% of BSBS undergraduate majors. To address the limited availability of undergraduate research positions, BSBS has developed alternative programs such as PILOT to provide substantial numbers of students with practical, hands-on training in the life sciences

Desulphurization of steel and pig iron

Metallurgical slag qualities must be defined by the whole complex of physico - chemical characteristics, such as an oxidative ability, optical basicity, sulphide capacity up to slag fluidity, its surface tension etc. The understanding of regulation of basic physico - chemical qualities of molten metals and slag depending on a chemical structure and a temperature has its importance at the level of the metallurgical process control. Presented paper deals with the possibilities how to exploit the sulphidic capacity for the desulphurisation evaluation in course of the metal reafining in the oxygen converter based on the set of the operational data. The integral part of the work is the process of the pig iron desulphurisation

Structural Dynamics of α-Actinin-Vinculin Interactions

α-Actinin and vinculin orchestrate reorganization of the actin cytoskeleton following the formation of adhesion junctions. α-Actinin interacts with vinculin through the binding of an α-helix (αVBS) present within the R4 spectrin repeat of its central rod domain to vinculin's N-terminal seven-helical bundle domain (Vh1). The Vh1:αVBS structure suggests that αVBS first unravels from its buried location in the triple-helical R4 repeat to allow it to bind to vinculin. αVBS binding then induces novel conformational changes in the N-terminal helical bundle of Vh1, which disrupt its intramolecular association with vinculin's tail domain and which differ from the alterations in Vh1 provoked by the binding of talin. Surprisingly, αVBS binds to Vh1 in an inverted orientation compared to the binding of talin's VBSs to vinculin. Importantly, the binding of αVBS and talin's VBSs to vinculin's Vh1 domain appear to also trigger distinct conformational changes in full-length vinculin, opening up distant regions that are buried in the inactive molecule. The data suggest a model where vinculin's Vh1 domain acts as a molecular switch that undergoes distinct structural changes provoked by talin and α-actinin binding in focal adhesions versus adherens junctions, respectively