Virus Structure And Assembly

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Publisher: Elsevier
ISBN: 0080455085
Size: 12.93 MB
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Virus Structure And Assembly by

Original Title: Virus Structure And Assembly

Written by experts in their field, Virus Structure and Assembly summarizes our current state of knowledge in the field of virus structure and assembly, comparing and contrasting the mechanisms adopted by viruses with a wide diversity of genome and host. It will serve as an invaluable reference for researchers in virology, microbiology, epidemiology, molecular biology, and public health. * Witness to the remarkable advancement in the field of virus structure and assembly * A unique opportunity to compare and contrast mechanisms adopted by a diverse range of viruses from bacteriophages and RNA viruses to Bluetongue, Influenza and Hepatitis B * Numerous illustrations including color * Discussion on the VIPER database, a repository for all high-resolution structures of simple icosahedral viruses, and on application of mass spectrometry to the analysis of structures present in biological specimens, such as HIV-1

Nanoscale Structure And Assembly At Solid Fluid Interfaces

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Author: James J. De Yoreo
Publisher: Springer
ISBN: 9781402078101
Size: 37.53 MB
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Nanoscale Structure And Assembly At Solid Fluid Interfaces by James J. De Yoreo

Original Title: Nanoscale Structure And Assembly At Solid Fluid Interfaces

The aim of this reference is to take us to the root of these issues: the solid-fluid interfacial structures and the basic interactions between structural units that determine the kinetics of nano particles and assembly formation, and subsequently the resulting structures and functionalities of the nano phases and devices. By taking a fresh look at the novel nano structure engineering and surface probing technologies from a global viewpoint of fundamental principles, the two volumes of this book direct our focus from the macroscopic phase to the nano structures ranging from inorganic to bio nano materials. Featuring contributions from a number of international experts in the related fields, this book offers a comprehensive and synergistic look into these challenging issues in terms of theoretical modeling, computer simulations, advanced surface probing and fabrication and interface characterizations. The book also provides a link to the nanostructure engineering of some novel materials playing an important role in advancing technologies in this field.

Comprehensive Virology Volume 13 Structure And Assembly

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Author: Heinz Fraenkel-Conrat
Publisher: Springer Science & Business Media
ISBN: 1468434535
Size: 25.60 MB
Format: PDF, Kindle
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Comprehensive Virology Volume 13 Structure And Assembly by Heinz Fraenkel-Conrat

Original Title: Comprehensive Virology Volume 13 Structure And Assembly

The time seems ripe for a critical compendium of that segment of the biological universe we call viruses. Virology, as a science, having passed only recently through its descriptive phase of naming and num bering, has probably reached that stage at which relatively few new-truly new-viruses will be discovered. Triggered by the intellectual probes and techniques of molecular biology, genetics, bio chemical cytology, and high resolution microscopy and spec troscopy, the field has experienced a genuine information explosion. Few serious attempts have been made to chronicle these events. This comprehensive series, which will comprise some 6000 pages in a total of about 18 volumes, represents a commitment by a large group of active investigators to analyze, digest, and expostulate on the great mass of data relating to viruses, much of which is now amorphous and disjointed, and scattered throughout a wide literature. In this way, we hope to place the entire field in perspective, and to develop an invalua ble reference and sourcebook for researchers and students at all levels. This series is designed as a continuum that can be entered anywhere, but which also provides a logical progression of developing facts and integrated concepts.

On The Structure And Assembly Of Staphylococcal Leukocidin

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Author: George Emmett Miles
Size: 36.26 MB
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On The Structure And Assembly Of Staphylococcal Leukocidin by George Emmett Miles

Original Title: On The Structure And Assembly Of Staphylococcal Leukocidin

Staphylococcal leukocidin pores are formed by the obligatory interaction of two distinct polypeptides, one of class F and one of class S, making them unique in the family of [beta]-barrel pore-forming toxins ([beta]-PFTs). By contrast, other [beta]-PFTs form homooligomeric pores. For example, the staphylococcal [alpha]-hemolysin is a homoheptamer. Limited and controversial data exist on the assembly and molecular architecture of the leukocidin pore. In this work, biochemical and biophysical methods were used to characterize the leukocidin pore produced by the LukF (HlgB) and LukS (HlgC) components encoded by Staphylococcus aureus. I demonstrate that LukF and LukS assemble to form an SDS-stable pore on rabbit erythrocyte membranes. In addition, the pore-forming properties of recombinant leukocidin were investigated with planar lipid bilayers. Although leukocidins and staphylococcal [alpha]-hemolysin share partial sequence identity and related folds, LukF and LukS produce a pore with a unitary conductance of 2.5 nS (1 M KCl, 5mM HEPES, pH 7.4), which is over three times greater than that of [alpha]-hemolysin measured under the same conditions. The subunit composition and stoichiometry of a leukocidin pore were determined by two independent methods, gel shift electrophoresis and site specific chemical modification during single channel recording. Four LukF and four LukS subunits were shown to co-assemble into an octameric transmembrane structure. The existence of an additional subunit in part explains properties of the leukocidin pore, such as its high conductance. Additionally, this is the first time that either technique has been applied successfully to assess the composition of a heteromeric membrane protein. It is also relevant to understanding the mechanism of assembly of [beta]-PFT pores, and suggests new possibilities for engineering these proteins. In additional studies, the HlyII pore encoded by Bacillus cereus was found to form a homoheptameric transmembrane pore with properties conforming ingeneral with those of other members of the class of [beta]-PFTs. HlyII possesses additional properties which make it an attractive candidate for applications in biotechnology, such as an oligomer with a high thermal stability in the presence of SDS and the ability of the pore to remain open at high transmembrane potentials.

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