Structure of the Phage T4 Tail Fiber Angle

Abstract

Our goal is to form a polygonal nanospring by self-assembly, from a designed strut-like chimeric protein. This protein is made from fragments of the T4 tail fiber and binds specifically to its angle protein. We have designed and expressed this chimeric protein which will inhibit the burst size of a T4 infected bacterium. This indicates that the chimeric protein can fold and oligomerize to create a site that binds tightly enough to the angle protein to sequester it and thereby greatly reduce the phage burst size.

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Document Details

Document Type
Technical Report
Publication Date
Jul 01, 2002
Accession Number
ADA403938

Entities

People

  • Edward Goldberg

Organizations

  • Tufts University

Tags

Communities of Interest

  • Biomedical

DTIC Thesaurus Topics

  • Abstracts
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  • Information Operations
  • Instructions
  • Manufacturing
  • Military Research
  • Molecular Biology
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  • Self Assembly
  • Terminals

Readers

  • Molecular Genetics
  • Molecular and Cellular Biochemistry
  • Optical Fiber Sensing and Electromagnetic Propagation.