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3 edition of Bacteriophage M13 major coat protein found in the catalog.

Bacteriophage M13 major coat protein

Bacteriophage M13 major coat protein

roles of aromatic residues at the membrane-water interface.

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Published by National Library of Canada in Ottawa .
Written in English


Edition Notes

Thesis (M.Sc.) -- University of Toronto, 1999.

SeriesCanadian theses = -- Thèses canadiennes
The Physical Object
FormatMicroform
Pagination2 microfiches : negative. --
ID Numbers
Open LibraryOL21878790M
ISBN 100612458822

M13 Major Coat Protein (RL-ph1) is a mouse monoclonal antibody raised against isolated M13 phage coat proteins. PRODUCT Each vial contains µg IgG 2b kappa light chain in ml of PBS with M13 Major Coat Protein (RL-ph1) is . CiteSeerX - Document Details (Isaac Councill, Lee Giles, Pradeep Teregowda): The M13 filamentous bacteriophage coat is a symmetric array of several thousand a-helical major coat proteins (P8) that surround the DNA core. P8 molecules initially reside in the host membrane and subsequently transition into their role as coat proteins during the phage assembly process.

EPI is the only known human protein that inhibits thrombin but unfortunately EPI has a low affinity and specificity for the protease. To possibly solve this problem, researchers have engineered a recombinant M13 phage that displays a modified version of the major coat protein that is fused with EPI at its N- . M13 is a virus that infects the bacterium Escherichia coli. It is composed of a circular single-stranded DNA molecule encased in a thin flexible tube made up of about copies of the major coat protein, P8. The ends of the tube are capped with minor coat proteins.

  Self assembles to form a helical capsid wrapping up the viral genomic DNA. The capsid displays a filamentous structure with a length of nm and a width of nm. The virion assembly and budding take place at the host inner membrane. We have reported variants of the M13 bacteriophage major coat protein ~P8! that enable high copy display of monomeric and oligomeric proteins, such as human growth hormone and steptavidin, on the surface of phage particles ~Sidhu SS, Weiss GA, Wells JA. High copy display of large proteins on phage for functional selections.


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Bacteriophage M13 major coat protein Download PDF EPUB FB2

Displayed elements are expressed on the surface of filamentous M13 bacteriophage typically as a fusion to either the major (pVIII) or minor (pIII) phage coat protein; the DNA of each library member is packaged within the phage particle, thus linking its phenotype with its genotype (Fig.

This critical phenotype-to-genotype linkage allows for. At least five phage-specific proteins, including the two coat proteins, are present in appreciable quantities in Minfected cells.

The principal phage protein synthesized is the product of gene 5, which is responsible for phage single-stranded DNA synthesis.

This protein Cited by:   The major coat protein is a small protein with a molecular weight of about Da and forms a –nm-thick flexible cylindrical shell. It is composed of three specific domains: a hydrophobic core, an acidic N-terminal, and a basic C-terminal part (see the primary sequence in Fig.

2).In the phage particle the major coat protein is largely α-helical with four to five flexible Cited by: Abstract. A method which allows one to follow the synthesis of the major f1 coat protein in normal, unirradiated f1-infected cells is reported.

The N-terminal tryptic peptide of this protein, labeled with 14 C-lysine, has a negative charge at pH and is readily separated from the contaminating peptides of host cell proteins.

This technique was used to study several aspects of the synthesis Cited by: Figure M13 genome. Gene VIII codes for the major structural protein of the bacteriophage particles; Gene III codes for the minor coat protein; Figure Gene III and gene VIII.

The gene VIII protein forms a tubular array of approx. 2, identical subunits surrounding the viral genome. Major coat protein. Gene. VIII. Organism. Enterobacteria phage M13 (Bacteriophage M13) Status. Unreviewed-Annotation score: Protein predicted i. Names & Taxonomy i. Protein names i: Submitted name: Major coat protein Imported.

Gene names i: Name:VIII Imported. Organism i. The filamentous M13 bacteriophage consists of a single-stranded DNA core surrounded by a proteinaceous coat. 1 The ends of the virus are capped by minor coat proteins, but the vast majority of the coat consists of several thousand copies of the gene-8 major coat protein (protein-8, P8).

P8 molecules cover the length of the filament in a repeating array, with N termini exposed on the surface. Anti-M13 Major Coat Protein Antibody (RL-ph1) is a mouse monoclonal IgG 2b (kappa light chain) M13 Major Coat Protein antibody provided at µg/ml; raised against isolated M13 phage coat proteins; M13 Major Coat Protein Antibody (RL-ph1) is recommended for detection of M13 /5(5).

*Corresponding author M13 bacteriophage Introduction M13 bacteriophage is a filamentous, Escherichia coli-specific virus approximately 1 mm in length but less than 10 nm in diameter. The viral filament consists of a circular, single-stranded DNA (ssDNA) core surrounded by a protein coat.1 The ends of the particle are capped by about five.

The structure and changes in environment of the M13 major coat protein were studied in model systems, mimicking the initial molecular process of the phage disassembly. For this purpose we have systematically studied protein associations with various detergents and lipids in two different coat protein assemblies: phage particles and S-forms.

2. M13 Bacteriophage-Based Protein and Microorganism Sensing. Indeed, using a natural M13 bacteriophage without any genetic engineering provides a great opportunity because of the abundant negative charge on the surface protein. The α-helical major coat protein (pVIII) has glutamate amino acid on the end of its sequence.

Phage display protein engineering combinatorial mutagenesis M13 bacteriophage major coat protein viral evolution This is a preview of subscription content, log in to check access. Springer Nature is developing a new tool to find and evaluate Protocols.

M13 is a filamentous bacteriophage composed of circular single stranded DNA (ssDNA) which is nucleotides long encapsulated in approximately copies of the major coat protein P8, and capped with 5 copies of two different minor coat proteins (P9, P6, P3) on the ends. The three-dimensional structure of the major coat protein of bacteriophage M13, solubilized in detergent micelles, has been determined using heteronuclear multidimensional NMR and restrained molecular dynamics.

The protein consists of two alpha-helices, running from residues 8 to 16 and 25 to 45, respectively. The filamentous M13 bacteriophage (M13 phage) contains a circular single-stranded DNA genome that encodes only 10 proteins.

The wild type genome is enclosed in a cylindrical protein coat consisting of copies of major coat protein, pVIII (UnitProtKB - P). At either end of the virion, there are a number of minor coat proteins. We have reported variants of the M13 bacteriophage major coat protein (P8) that enable high copy display of monomeric and oligomeric proteins, such as human growth hormone and steptavidin, on the surface of phage particles (Sidhu SS, Weiss GA, Wells JA.

High copy display of large proteins on phage for functional selections. CiteSeerX - Document Details (Isaac Councill, Lee Giles, Pradeep Teregowda): A peptide was fused to the C terminus of the M13 bacteriophage major coat protein (P8), and libraries of P8 mutants were screened to select for variants that displayed the peptide with high efficiency.

Over variants were sequenced to compile a comprehensive database of P8 sequence diversity compatible with. Most of the M13 particles were eluted as a single sharp peak with a retention time at min.

The SDS-PAGE of the fraction at this peak revealed a highly purified band of the major coat protein of M13 with purity comparable to that of CsCl gradient density ultracentrifugation purified M Download: Download full-size image. Abstract.

The membrane insertion of bacteriophage coat proteins occurs independent of the Sec-translocase of Escherichia ed study of the Pf3 and M13 coat proteins has elucidated two fundamental mechanisms of how proteins invade the membrane.

Phage display is a laboratory technique for the study of protein–protein, protein–peptide, and protein–DNA interactions that uses bacteriophages (viruses that infect bacteria) to connect proteins with the genetic information that encodes them.

In this technique, a gene encoding a protein of interest is inserted into a phage coat protein gene, causing the phage to "display" the protein on. Here we generate a mutant version of M13 with an additional lysine residue expressed on the outer surface of the M13 major coat protein, pVIII.

We show that this mutation is accommodated by the bacteriophage and that up to an additional exogenous groups can be attached to the bacteriophage surface via amine-directed conjugation.In molecular biology, a phage major coat protein is an alpha-helical protein that forms a viral envelope of filamentous bacteriophages.

These bacteriophages are flexible rods, about one to two micrometres long and six nm in diameter, with a helical shell of protein subunits surrounding a DNA core.M13 Major Coat Protein (RL-ph1): The filamentous bacteriophage major coat protein occurs as a membrane-spanning assembly intermediate prior to incorporation into the lipid-free virion.

Assembly of coliphage M13 is known to occur as the viral DNA crosses the cytoplasmic membrane, shedding its virus-coded DNA unwinding protein and acquiring /5(5).