Size matters for the tripeptidylpeptidase II complex from drosophila: The 6-MDa spindle form stabilizes the activated state

Journal of Biological Chemistry

Volumn 281, Issue 35, 2006, Pages 25723-25733

  Seyit, Gönül ^a   Rockel, Beate ^a   Baumeister, Wolfgang ^a   Peters, Jürgen ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; DIMERS; GROWTH KINETICS; MOLECULAR BIOLOGY; POLYPEPTIDES; THERMODYNAMICS;

HOMOOLIGOMERIC COMPLEX; PROTEIN DEGRADATION; TRIPEPTIDYLPEPTIDASE II (TPP II);

ENZYMES;

EXOPEPTIDASE; INSECT PROTEIN; TRIPEPTIDYLPEPTIDASE II COMPLEX; UNCLASSIFIED DRUG;

ARTICLE; CONCENTRATION (PARAMETERS); CONFORMATIONAL TRANSITION; DROSOPHILA; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME STABILITY; ENZYME STRUCTURE; ESCHERICHIA COLI; MITOSIS SPINDLE; MOLECULAR WEIGHT; NONHUMAN; PARTICLE SIZE; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN MOTIF; THERMODYNAMICS;

ANIMALS; CLONING, MOLECULAR; CROSS-LINKING REAGENTS; DENSITOMETRY; DIMERIZATION; DOSE-RESPONSE RELATIONSHIP, DRUG; DROSOPHILA; ESCHERICHIA COLI; KINETICS; PEPTIDE HYDROLASES; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SERINE ENDOPEPTIDASES; THERMODYNAMICS; TIME FACTORS;

ESCHERICHIA COLI; EUKARYOTA;

EID: 33748750830     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M602722200     Document Type: Article

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