Literature DB >> 1959617

A model for fd phage penetration and assembly.

A K Dunker1, L D Ensign, G E Arnold, L M Roberts.   

Abstract

Below 15 degrees C, chloroform causes fd phage to contract to I-forms, which are compact structures about 1/3 as long as the original phage. Above 15 degrees C, chloroform causes I-forms to contract to even more compact spheroidal S-forms. Here we show that the coat protein structure in I-forms is the same as the protein structure in the phage and the protein structure in S-forms is the same as the protein structure in bilayers. The conversions from fd----I-forms----S-forms are therefore suggested to mimic steps in fd penetration. The same conversions, in reverse order, are suggested to mimic steps in fd assembly.

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Year:  1991        PMID: 1959617     DOI: 10.1016/0014-5793(91)80882-4

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

Review 1.  Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function.

Authors:  Ursula Jakob; Richard Kriwacki; Vladimir N Uversky
Journal:  Chem Rev       Date:  2014-02-06       Impact factor: 60.622

2.  Val-->Ala mutations selectively alter helix-helix packing in the transmembrane segment of phage M13 coat protein.

Authors:  C M Deber; A R Khan; Z Li; C Joensson; M Glibowicka; J Wang
Journal:  Proc Natl Acad Sci U S A       Date:  1993-12-15       Impact factor: 11.205

  2 in total

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