عنوان

Bacteriophage T4 tail fibers as a basis for structured assemblies

شابک

9781606506868

شابک اشتباه

9781606506851

شماره

b398665

عنوان اصلي

Bacteriophage T4 tail fibers as a basis for structured assemblies

نام عام مواد

[Book]

نام نخستين پديدآور

by Paul Hyman and Timothy Harrah.

نام خاص و کميت اثر

1 online resource (xiii, 84 pages) :

ساير جزييات

illustrations.

عنوان فروست

Biomedical & nanomedical technologies

متن يادداشت

Co-published with American Society of Mechanical Engineers.

متن يادداشت

Includes bibliographical references (pages 73-82) and index.

متن يادداشت

1. Introduction --

متن يادداشت

2. Tail fiber function and structure -- 2.1 Hypothesis -- 2.2 Staged or ordered assembly -- 2.3 Possible applications --

متن يادداشت

3. Tail fiber production and purification --

متن يادداشت

4. Tail fiber modifications -- 4.1 Deletions and insertions -- 4.2 Coiled-coil assembly segment modifications -- 4.2.1 Biological role of the gp 37 coiled-coil -- 4.2.2 Coiled-coils as intrinsic chaperones -- 4.3 Inserts conferring novel functionality -- 4.3.1 Insertion and testing of an antibody binding epitope -- 4.3.2 Insertion and testing of a biotinylation site -- 4.3.3 Attaching magnetic nanoparticles via a biotin linkage -- 4.3.4 Potential tail fiber-nanoparticle system improvements --

متن يادداشت

5. Conclusions -- Appendices -- A. Tail fiber purification -- B. Preparation of head-tail (HT) complexes -- C. Purified tail fiber assay -- D. Analytical ultracentrifugation -- E. Electron microscopy -- F. Bacteria and bacteriophage strains -- G. Media and buffers -- H. Phage stock growth and construction of phage with multiple mutations -- I. Transfer of engineered mutations into phage -- J. PCR and sequencing primers -- K. Adsorption rate measurements -- L. Construction of extended coiled-coil region -- M. Mab binding assays -- N. Construction of biotinylated phage -- O. Western blot and SDS-PAGE analysis -- P. Purification of biotinylated tail fibers -- Q. Preparation of nanoparticles -- R. Attachment of nanoparticles to biotinylated tail fibers -- S. Dynamic light scattering (DLS) -- T. AC magnetic susceptometry theory -- U. Magnetic susceptibility measurements -- About the authors -- References -- Index.

بدون عنوان

0

بدون عنوان

8

بدون عنوان

8

بدون عنوان

8

بدون عنوان

8

متن يادداشت

Bacteriophages, viruses that infect bacteria, have evolved a variety of complex protein structures to carry their genomes between host cells. These proteins form the virion particle which can be considered a mostly self-assembled protein machine that protects the genome and effects genome entry into new cells. Because bacteriophages (phages) are often found in harsh environments including animal digestive tracts, sewage, and sea water, virion particle proteins are typically very stable and resistant to changes in pH, salts, digestive proteases, and other agents that typically denature or degrade proteins. Bacteriophage T4 long tail fibers are specialized proteins that bind to the host cell surface. They are very long (.160 nm) and thin (.3-5 nm) rigid fibrous multiprotein structures. The high length to width ratio of the long tail fibers (LTFs), rigidity, self-assembling properties plus chemical durability suggest that LTFs could be adapted into a self-patterning nanoscale protein structure or system. Although crystallizing whole tail fibers remains a challenge, structural data on fiber fragments, related trimeric protein fibers, and other data suggest that some type of repetitive beta secondary structure comprises part of the rigid rod portions of the tail fibers. The presence of segments of beta structure arising from mostly local interactions also support the proposition that tail fibers can withstand a variety of modifications without compromising the overall structure and function of the bacteriophage. Toward the goal of creating structured assemblies we have constructed and tested a variety of tail fibers with alterations in gp 37, which forms the distal end of the native tail fiber, as well as developed an improved purification method for the assembled tail fiber. The alterations include deletions to reduce the overall length and modifications to a key segment where assembly is initiated to improve assembly in vitro. We have also added a variety of attachment sites to several locations in the gp 37 including a biotinylation site and an antibody binding epitope. These insertions do not appear to disrupt the gp 37 structure in any way and phages carrying these gp 37 modifications remain viable. In this monograph, we will review what is known about the structure of the bacteriophage T4 tail fiber system and present a model of how it can be adapted into a controlled self-assembling system. We further review the published and unpublished work we have completed on tail fiber purification and modifications.

شماره استاندارد بين المللي کتاب و موسيقي

9781606506851

موضوع مستند نشده

Bacteriophage T4.

موضوع مستند نشده

Biomimetic materials.

موضوع مستند نشده

Nanobiotechnology.

مستند نام اشخاص تاييد نشده

Hyman, Paul

مستند نام اشخاص تاييد نشده

Harrah, Timothy

تاريخ عمليات

20190122105700.0

قواعد فهرست نويسي ( بخش توصيفي )

rda

نام الکترونيکي

نوع ماده

[Book]

تكميل شده

Y