Association and dissociation of the cell puncturing complex of bacteriophage T4 is controlled by both pH and temperature

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1764, Issue 9, 2006, Pages 1487-1492

  Kumar Sarkar, Subodh ^a   Takeda, Yoko ^a   Kanamaru, Shuji ^a   Arisaka, Fumio ^a  

^a TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

Author keywords

Bacteriophage T4; Infection; Processing; Sedimentation equilibrium; Structure; Tail lysozyme

Indexed keywords

ALANINE; LYSOZYME; MONOMER; PEPTIDOGLYCAN; PROTEIN SUBUNIT; SERINE;

AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIOPHAGE; CELL ACTIVITY; CELL MEMBRANE; COMPLEX FORMATION; CYTOPLASM; DISSOCIATION; HEATING; INFECTION; NONHUMAN; PH MEASUREMENT; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN INTERACTION; PROTEIN STRUCTURE; TEMPERATURE DEPENDENCE;

BACTERIOPHAGE T4; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MURAMIDASE; PROTEIN STRUCTURE, QUATERNARY; TEMPERATURE; ULTRACENTRIFUGATION; VIRAL PROTEINS; VIRAL TAIL PROTEINS;

EID: 33748468237     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2006.07.007     Document Type: Article

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