Domain:domain interactions within Hop, the Hsp70/Hsp90 organizing protein, are required for protein stability and structure

Protein Science

Volumn 15, Issue 3, 2006, Pages 522-532

  Carrigan, Patricia E ^a   Sikkink, Laura A ^a   Smith, David F ^a   Ramirez Alvarado, Marina ^a  

^a MAYO GRADUATE SCHOOL   (United States)

Author keywords

Chaperonins; Circular dichroism; Protein structure folding; Tetratricopeptide repeat

Indexed keywords

CARBOXYLIC ACID; CHAPERONE; CHAPERONE HOP; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; UNCLASSIFIED DRUG;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONFORMATION; PH; POINT MUTATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; WILD TYPE;

BINDING SITES; CIRCULAR DICHROISM; HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HSP90 HEAT-SHOCK PROTEINS; LIGANDS; PEPTIDES; POINT MUTATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; REPETITIVE SEQUENCES, AMINO ACID;

EID: 33644500163     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.051810106     Document Type: Article

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