Interactions between coat and scaffolding proteins of phage P22 are altered in vitro by amino acid substitutions in coat protein that cause a cold-sensitive phenotype.

doi:10.1021/bi960860l

Back to search

Article

Interactions between coat and scaffolding proteins of phage P22 are altered in vitro by amino acid substitutions in coat protein that cause a cold-sensitive phenotype.

Biochemistry - 26 Nov 1996

Teschke C M, Fong D G

Abstract excerpt

Cold-sensitive mutations in phage P22 coat protein cause the accumulation of precursor capsids in cells growing at the nonpermissive temperature (16 degrees C). The assembly of coat proteins which carry the substitutions threonine at position 10 to isoluecine (T10I), arginine at position 101 to c...

Topics

Amino Acids
Bacteriophage P22
Capsid
Cold Temperature
Mutation
Phenotype
Protein Binding
Protein Conformation
Protein Folding
Viral Proteins

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.