Stability of Bacteriophage T4 Short Tail Fiber
- 14 March 2000
- journal article
- Published by Walter de Gruyter GmbH in Biological Chemistry
- Vol. 381 (3) , 255-258
- https://doi.org/10.1515/bc.2000.032
Abstract
Adsorption of Teven 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 78C. Guanidinium chlorideinduced denaturation displayed strong hysteresis and an intermediate between 2 and 3 denaturant. The transitions occur at 1.5 and 3.2 denaturant as revealed by fluorescence spectroscopy and circular dichroism. The data suggest an equilibrium unfolding intermediate with a separate unfolding of the Cterminal knob domain and the shaft region.Keywords
This publication has 15 references indexed in Scilit:
- Thermal Unfolding of Bacteriophage T4 Short Tail FibersBiotechnology Progress, 1997
- Prediction of Protein Secondary Structure at Better than 70% AccuracyJournal of Molecular Biology, 1993
- The Short Tail-Fiber of Bacteriophage T4: Molecular Structure and a Mechanism for Its Conformational TransitionVirology, 1993
- New triple-helical model for the shaft of the adenovirus fibreJournal of Molecular Biology, 1992
- In vitro folding pathway of phage P22 tailspike proteinBiochemistry, 1991
- Receptor specificity of the short tail fibres (gp12) of T-even type Escherichia coli phagesMolecular Genetics and Genomics, 1987
- [14]Determination and analysis of urea and guanidine hydrochloride denaturation curvesPublished by Elsevier ,1986
- Bacteriophage T4 short tail fibers are the product of gene 12Journal of Molecular Biology, 1974
- Product of T4 gene 12Journal of Molecular Biology, 1972
- Polypeptides of the tail fibres of bacteriophage T4Journal of Molecular Biology, 1971