Protein toxin structure

  • 309 Pages
  • 1.20 MB
  • 847 Downloads
  • English

Springer, R.G. Landes , New York, Austin
Toxins -- Structure-activity relations
Statement[edited by] Michael W. Parker.
SeriesMolecular biology intelligence unit, Molecular biology intelligence unit (Unnumbered)
ContributionsParker, Michael W., 1959-
Classifications
LC ClassificationsQP631 .P76 1996
The Physical Object
Pagination309 p. :
ID Numbers
Open LibraryOL984033M
ISBN 103540611916, 157059368X, 3540611916
LC Control Number96021770

Protein toxins possess AB structure-function organization, where the A domain encodes a catalytic function for the posttranslational modification of a host macromolecule, including proteins and nucleic acids, and a B domain, which encodes host receptor recognition, including proteins and glycosphingolipids, alone or in combination.

Protein. Open Library is an open, editable library catalog, building towards a web page for every book ever published. Protein Toxin Structure by Michael W. Parker,Parker Michael W, Springer edition, paperback. Read "Protein Toxin Structure" by available from Rakuten Kobo. pleased to have the opportunity to briefly highlight some important issues relevant to structural aspects of bacterial protein tox ins.

The present book attempts for the first time to provide into one volume a series of chapters prepared by invited experts on the struc ture of Brand: Springer Berlin Heidelberg.

Open Library is an open, editable library catalog, building towards a web page for every book ever published. Protein Toxin Structure by Michael W. Parker; 1 edition; First published in Protein Toxin Structure | Open Library.

Protein Toxin Structure (Molecular Biology Intelligence Unit) Softcover reprint of the original 1st ed. Edition. by Michael W. Parker (Author) ISBN ISBN Why is ISBN important. ISBN. This bar-code number lets you verify that you're getting exactly the right version or edition of a book.

Author: Michael W. Parker. Protein Toxin Structure. Editors: Parker, Michael W. (Ed.) Free Preview. Buy this book eB29 € price for Spain (gross) Buy eBook ISBN ; Digitally watermarked, DRM-free; Included format: EPUB, PDF; ebooks can be used Protein toxin structure book all reading.

Protein Toxin Structure. Authors (view affiliations) pleased to have the opportunity to briefly highlight some important issues relevant to structural aspects of bacterial protein tox­ ins. The present book attempts for the first time to provide into one volume a series of chapters prepared by invited experts on the struc­ ture of these.

COVID Resources. Reliable information about the coronavirus (COVID) is available from the World Health Organization (current situation, international travel).Numerous and frequently-updated resource results are available from this ’s WebJunction has pulled together information and resources to assist library staff as they consider how to handle coronavirus.

Four sections cover protein structure, enzymes, special proteins, and membrane transport. There are brief problem sets following chapters, short bios of notable protein scientists, and references and an index provided in the appendices of the textbook.

This book describes the major achievements and discoveries relevant to bacterial protein toxins since the turn of the new century illustrated by the discovery of more than fifty novel toxins (many of them identified through genome screening).

Wasabi receptor toxin (WaTx) is the active component of the venom of the Australian black rock scorpion Urodacus targets TRPA1, also known as the wasabi receptor or irritant receptor.

WaTx is a cell-penetrating toxin that stabilizes the TRPA1 channel open state while reducing its Ca 2+-permeability, thereby eliciting pain and pain hypersensitivity without the neurogenic Class: Small protein.

Botulinum toxin (Botox) is a neurotoxic protein produced by the bacterium Clostridium botulinum and related species.

Details Protein toxin structure PDF

It prevents the release of the neurotransmitter acetylcholine from axon endings at the neuromuscular junction and thus causes flaccid paralysis. Infection with the bacterium causes the disease toxin is also used commercially for medical and cosmetic status: US: ℞-only.

Protein Purification Protein mixtures can be fractionated by chromatography. Proteins and other charged biological polymers migrate in an electric field. Primary Structure of Proteins The amino acid sequence or primary structure of a purified protein can be determined. Polypeptide sequences can be obtained from nucleic acid Size: 2MB.

Fundamentals of Protein Structure and Function. Engelbert Buxbaum, Dr. rer. nat. This book serves as an introduction to the fundamentals of protein structure and function.

Starting with their make up from simple building blocks called amino acids, the 3-dimensional structure of proteins is explained. The AB 5 toxin is a group of polypeptide chains, also known as a protein complex that pathogenic bacteria secrete in order to assist in overtaking a host.

The protein complex is composed of six components; five "B" Subunits (binds to the glycan receptors on the host cell) and one "A" subunit (the toxic subportion that disrupts host functions). Protein Toxin Structure. por.

Molecular Biology Intelligence Unit ¡Gracias por compartir. Has enviado la siguiente calificación y reseña. Lo publicaremos en nuestro sitio Brand: Springer Berlin Heidelberg. Cholera toxin was the first bacterial toxin visualized in the Golgi apparatus.

Later, toxin transport to the Golgi apparatus has been demonstrated for several other protein toxins as well. Both bacterial toxins and plant toxins such as ricin are transported from endosomes to the Golgi apparatus.

The Comprehensive Sourcebook of Bacterial Protein Toxins, Fourth Edition, contains chapters written by internationally known and well-respected book contains chapters devoted to individual toxins, as well as chapters that consider the different applications of these toxins.

Protein Toxin Structure (Molecular Biology Intelligence Unit) by Parker. Chapman & Hall. Used - Good. Former Library book. Shows some signs of wear, and may have some markings on the inside.

This book describes the strategies employed by protein toxins to render their pro- and eukaryotic producers a selective growth advantage over competitors. In providing an up-to-date overview on the mode of protein toxin actions, it accommodates biomedically and. Introducing a new cutting edge book on protein structure and function that is an ideal introduction for students and a must for all reading lists.

Protein Structure and Function considers the key concepts of protein structure and function and the relationship between sequence, structure and function with clear, concise explanations and full colour illustrations/5(3).

In light of the growing evidence in structural biology, it would be appropriate to suggest that protein dynamics and flexibility play a much bigger role in the function of the toxin than the structure itself.

In recent years remarkable progress has been accomplished with respect to our knowledge about bacterial protein toxins. This refers especially to structural aspects of protein toxins but also holds true for genetics, molecular biology and biochemical mechanisms underlying the action of toxins.

Description Protein toxin structure EPUB

This. Abstract. Toxin complex (Tc) proteins are a class of bacterial protein toxins that form large, multisubunit complexes. Comprising TcA, B, and C components, they are of great interest because many exhibit potent insecticidal activity.

The determination of the structure of the protein, called Community Acquired Respiratory Distress Syndrome (CARDS) toxin, will facilitate drug and vaccine development in. Abstract. The structure of Msmeg_, a protein of unknown function, has been determined.

Biochemical and bioinformatics analyses determined that Msmeg_ interacts with a protein encoded in the same operon, Msmeg_, and predicted that the operon is a toxin–antitoxin (TA) system. Book January is the most complex bacterial toxin known today.

It is a multimeric protein with a total molecular mass of kDa and is composed of five dissimilar subunits (Fig. The pathogen Clostridium difficile colonizes the human colon when the normal microbiota is disrupted, often after antibiotic treatment.

It is a leading cause of hospital-acquired diarrhea, especially among elderly patients. Chen et al. describe a Å-resolution crystal structure that shows how a major virulence factor in C. difficile, toxin B (TcdB), binds to the G protein–coupled Cited by: Shiga toxin (Stx) is one of the most potent bacterial toxins known.

Stx is found in Shigella dysenteriae 1 and in some serogroups of Escherichia coli (called Stx1 in E. coli). In addition to or instead of Stx1, some E. coli strains produce a second type of Stx, Stx2, that has the same mode of action as Stx/Stx1 but is antigenically by: Resolving the three dimensional structure of a protein is a critical step in modern drug discovery today.

Homology modeling is a powerful tool that can efficiently predict protein structures from Author: Pascal Gagneux. Bacterial toxins play an important role in infectious diseases. Several are amongst the most potent biological agents known to man.

Cholera, pertussis, botulinum, clostridium and tetanus toxins are all produced by bacteria. In many cases, it is the toxin produced and not the infectious agent itself that causes pathology. Botulinum toxin has now of course found clinical application as botox.ISBN: OCLC Number: Description: xxiii, pages: illustrations ; 29 cm: Contents: Ch.

1. A year story of bacterial protein toxins (): from "diphtheritic poison" to molecular toxinology --Ch. ionary aspects of toxin-producing bacteria --Ch. genetic elements and pathogenicity islands encoding bacterial toxins --Ch.

Download Protein toxin structure EPUB

4.A C-terminal toxin domain carried by an extended Hcp exhibited antibacterial effect. Previous studies demonstrated that each T6SS can possess more than one cognate Hcp, VgrG, or PAAR-repeat protein. 31,32 The VgrG and PAAR proteins have been demonstrated to carry diverse C-terminal extension domains functioning as T6SS antibacterial effectors, 6,16,32 while the toxic domains fused to Hcp.