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Tryptophan Residues Are Critical for Portal Protein Assembly and Incorporation in Bacteriophage P22

Tryptophan Residues Are Critical for Portal Protein Assembly and Incorporation in Bacteriophage P22

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_e9045634e7dd4872a8e106b9a7a8c50f

Tryptophan Residues Are Critical for Portal Protein Assembly and Incorporation in Bacteriophage P22

About this item

Full title

Tryptophan Residues Are Critical for Portal Protein Assembly and Incorporation in Bacteriophage P22

Publisher

Switzerland: MDPI AG

Journal title

Viruses, 2022-06, Vol.14 (7), p.1400

Language

English

Formats

Publication information

Publisher

Switzerland: MDPI AG

More information

Scope and Contents

Contents

The oligomerization and incorporation of the bacteriophage P22 portal protein complex into procapsids (PCs) depends upon an interaction with scaffolding protein, but the region of the portal protein that interacts with scaffolding protein has not been defined. In herpes simplex virus 1 (HSV-1), conserved tryptophan residues located in the wing doma...

Alternative Titles

Full title

Tryptophan Residues Are Critical for Portal Protein Assembly and Incorporation in Bacteriophage P22

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_e9045634e7dd4872a8e106b9a7a8c50f

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_e9045634e7dd4872a8e106b9a7a8c50f

Other Identifiers

ISSN

1999-4915

E-ISSN

1999-4915

DOI

10.3390/v14071400

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