Conformational stability of P22 tailspike proteins carrying temperature-sensitive folding mutations.

doi:10.1021/bi00469a022

Back to search

Article

Conformational stability of P22 tailspike proteins carrying temperature-sensitive folding mutations.

Biochemistry - 1 May 1990

Thomas G J, Becka R, Sargent D, Yu M H, King J

Abstract excerpt

The thermostable tailspike endorhamnosidase of Salmonella phage P22 provides a model system for comparing the role of amino acid sequences in determining the intracellular folding pathway with their role in stabilizing the mature structural protein. Complete Raman band assignments are given here...

Topics

Amino Acid Sequence
Molecular Sequence Data
Mutation
Protein Conformation
Protein Denaturation
Salmonella
Salmonella Phages
Spectrum Analysis, Raman
Temperature
Viral Proteins
Viral Tail 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.