Inter-ring communication allows the GroEL chaperonin complex to distinguish between different substrates

Protein Science

Volumn 16, Issue 5, 2007, Pages 956-965

  Van Duijn, Esther ^a,b   Heck, Albert J R ^b   Van Der Vies, Saskia M ^a  

^a VU UNIVERSITY AMSTERDAM   (Netherlands)

^b UTRECHT UNIVERSITY   (Netherlands)

Author keywords

Bacteriophage T4; Capsid proteins; Native mass spectrometry; Protein folding; Substrate binding

Indexed keywords

CAPSID PROTEIN; CHAPERONIN; MALATE DEHYDROGENASE; PROTEIN GP23; PROTEIN GP5; RIBULOSEBISPHOSPHATE CARBOXYLASE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIOPHAGE T4; BINDING AFFINITY; COLLISIONALLY ACTIVATED DISSOCIATION; COMPLEX FORMATION; CONTROLLED STUDY; ELECTROSPRAY; ESCHERICHIA COLI; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; TANDEM MASS SPECTROMETRY;

BACTERIOPHAGE T4; CAPSID PROTEINS; GROEL PROTEIN; PROTEIN BINDING; PROTEIN FOLDING; SUBSTRATE SPECIFICITY; TANDEM MASS SPECTROMETRY;

ESCHERICHIA COLI; MIRIDAE;

EID: 34247616673     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062713607     Document Type: Article

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