Structural studies of the contractile tail sheath protein of bacteriophage T4. 2. Structural analyses of the tail sheath protein, gp18, by limited proteolysis, immunoblotting and immunoelectron microscopy
- 1 May 1990
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 29 (21) , 5057-5062
- https://doi.org/10.1021/bi00473a009
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 9 references indexed in Scilit:
- Structural studies of the contractile tail sheath protein of bacteriophage T4. 1. Conformational change of the tail sheath upon contraction as probed by differential chemical modificationBiochemistry, 1990
- Analysis of near-neighbor contacts in bacteriophage T4 wedges and hubless baseplates by using a cleavable chemical cross-linkerJournal of Virology, 1989
- Nucleotide sequence of the tail sheath gene of bacteriophage T4 and amino acid sequence of its productJournal of Virology, 1988
- Potential length determiner and dna injection protein is extruded from bacteriophage T4 tail tubes in vitroVirology, 1986
- Three-dimensional structure of unstained, frozen-hydrated extended tails of bacteriophage T4Journal of Molecular Biology, 1985
- Studies of the structure of the T4 bacteriophage tail sheathJournal of Molecular Biology, 1976
- The infection of Escherichia coli by T2 and T4 bacteriophages as seen in the electron microscope II. Structure and function of the baseplateVirology, 1967
- Structure of the sheath of bacteriophage T4Journal of Molecular Biology, 1967
- On the fine structure of normal and “Polymerized” tail sheath of phage T4Journal of Ultrastructure Research, 1964