Properties of bacteriophage T4 baseplate protein encoded by gene 8

Autor:	M M, Shneider, S P, Boudko, A, Lustig, V V, Mesyanzhinov
Rok vydání:	2001
Předmět:	Viral Proteins Base Sequence Genes Viral Circular Dichroism Molecular Sequence Data Bacteriophage T4 Electrophoresis Polyacrylamide Gel Amino Acid Sequence Cloning Molecular Ultracentrifugation Protein Structure Secondary Recombinant Proteins Glycoproteins
Zdroj:	Biochemistry. Biokhimiia. 66(6)
ISSN:	0006-2979
Popis:	Gene product 8 (gp8, 344 amino acids per monomer) of bacteriophage T4 is one of the baseplate structural proteins. We constructed an expression vector of gp8 and developed a method for purification of recombinant protein. CD spectroscopy showed that gp8 is an alpha/beta type structural protein. Its polypeptide chain consists of nearly 40% beta-structure and 15% alpha-helix. These data agree with results of prediction of secondary structure based on the amino acid sequence of the protein. The sedimentation coefficient under standard conditions (S20,w) is 4.6S. Analytical ultracentrifugation results demonstrated that gp8 in solution has two types of oligomers--dimer and tetramer. The tetramer of gp8 may be included in the wedge (1/6 of the baseplate), and the dimer may be an intermediate product of association.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::670fff1f158f972d8f1552a2a55a0fb6 https://pubmed.ncbi.nlm.nih.gov/11421820 Zobrazit plný text záznamu Full text from SpringerLink