Unfolding of bacteriophage P22 tailspike protein: enhanced thermal stability of an N-terminal fusion mutant
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(98)00876-X/fullpdf
Reference21 articles.
1. Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors.
2. Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 Å, fully refined structure of the endorhamnosidase at 1.56 Å resolution, and the molecular basis of O-antigen recognition and cleavage
3. Mechanism of phage P22 tailspike protein folding mutations
4. Crystal Structure of P22 Tailspike Protein: Interdigitated Subunits in a Thermostable Trimer
5. Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail spike protein
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