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Stability of Bacteriophage T4 Short Tail Fiber
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Martin R. Burda
Veröffentlicht/Copyright:
1. Juni 2005
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.
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Published Online: 2005-06-01
Published in Print: 2000-03-14
Copyright © 2000 by Walter de Gruyter GmbH & Co. KG
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Artikel in diesem Heft
- Interaction of E. coli Single-Stranded DNA Binding Protein (SSB) with Exonuclease I. The Carboxy-Terminus of SSB Is the Recognition Site for the Nuclease
- p38/SAPK2-Dependent Gene Expression in Jurkat T Cells
- The First Laminin G-Type Domain in the SHBG-Like Region of Protein S Contains Residues Essential for Activation of the Receptor Tyrosine Kinase Sky
- Permutation of the Active Site Motif of Tryparedoxin 2
- Structural Investigations of the Highly Flexible Recombinant Ribosomal Protein L12 from Thermotoga maritima
- Polyhistidine-Tagged Hepatitis B Core Particles as Carriers of HIV-1/gp120 Epitopes of Different HIV-1 Subtypes
- In Vitro Evolution of Ligands for HCV-Specific Serum Antibodies
- Stability of Bacteriophage T4 Short Tail Fiber
- Analysis of the RNase T1 Mediated Cleavage of an Immobilized Gapped Heteroduplex via Fluorescence Correlation Spectroscopy
- Binding of Selenoprotein P to Heparin: Characterization with Surface Plasmon Resonance
- Biotin-Avidin Microplate Assay for the Quantitative Analysis of Enzymatic Methylation of DNA by DNA Methyltransferases
