Pressure dissociation studies provide insight into oligomerization competence of temperature-sensitive folding mutants of P22 tailspike

Protein Science

Volumn 13, Issue 6, 2004, Pages 1538-1546

  Lefebvre, Brian G ^a   Comolli, Noelle K ^a   Gage, Matthew J ^a   Robinson, Anne Skaja ^a  

^a University of Delaware   (United States)

Author keywords

Aggregation; Hydrostatic pressure; P22 tailspike; Protein folding kinetics; Temperature sensitive mutations

Indexed keywords

BACTERIAL PROTEIN; MONOMER; PROTEIN P22 TAILSPIKE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACTERIOPHAGE P22; DISSOCIATION; HYDROSTATIC PRESSURE; LOW TEMPERATURE; MUTATION; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; TEMPERATURE SENSITIVE MUTANT; WILD TYPE;

BACTERIOPHAGE P22; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; PRESSURE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN RENATURATION; TEMPERATURE; VIRAL TAIL PROTEINS;

BACTERIA (MICROORGANISMS);

EID: 2442637627     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03579304     Document Type: Article

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