Literature DB >> 6793359

Purification, properties and assembly of the neck-appendage protein of the Bacillus subtilis phage phi 29.

N Villanueva, J M Lázaro, M Salas.   

Abstract

The purification of the neck appendage protein of phi 29, p12*, which is involved in the adsorption of the phage to Bacillus subtilis, is described. The purified native protein is in a dimeric form and can be assembled, in vitro, onto purified 12- particles that lack the neck appendages, suggesting that the incorporation of p12* to the rest of the phage structure is a self-assembly process. The assembly of protein p12* in vitro follows cooperative kinetics and it occurs with an efficiency of about 4%.

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Year:  1981        PMID: 6793359     DOI: 10.1111/j.1432-1033.1981.tb06365.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  1 in total

1.  Approaches to determine stoichiometry of viral assembly components.

Authors:  M Trottier; P Guo
Journal:  J Virol       Date:  1997-01       Impact factor: 5.103

  1 in total

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