title: Stability of bacteriophage T4 short tail fiber.
abstract: Adsorption of T-even bacteriophages to the E. coli host cell is mediated by long and short tail fibers. Bacteriophage T4 short tail fiber protein p12 was used to investigate the stability against thermal and chemical denaturation. Purified p12 is thermostable with a melting point of 78 degrees C. Guanidinium chloride-induced denaturation displayed strong hysteresis and an intermediate between 2 and 3 M denaturant. The transitions occur at 1.5 and 3.2 M denaturant as revealed by fluorescence spectroscopy and circular dichroism. The data suggest an equilibrium unfolding intermediate with a separate unfolding of the C-terminal knob domain and the shaft region.
authors.affiliation: Max-Planck-Institut für Biologie, Abteilung Mikrobiologie, Tübingen, Germany.
authors.forename: M R
authors.initials: MR
authors.lastname: Burda
authors.forename: I
authors.initials: I
authors.lastname: Hindennach
authors.forename: S
authors.initials: S
authors.lastname: Miller
mesh_terms: D000327:Adsorption; D000595:Amino Acid Sequence; D017122:Bacteriophage T4; D002942:Circular Dichroism; D019791:Guanidine; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D013050:Spectrometry, Fluorescence; D014764:Viral Proteins
chemical_list: D014764:Viral Proteins; C071684:gene 12 protein, Enterobacteria phage T4; D019791:Guanidine