Random circular permutation leading to chain disruption within and near α helices in the catalytic chains of aspartate transcarbamoylase: Effects on assembly, stability, and function

Protein Science

Volumn 10, Issue 3, 2001, Pages 528-537

  Beernink, Peter T ^a,b   Yang, Ying R ^a   Graf, Roney ^a,c   King, David S ^a   Shah, Shaival S ^a   Schachman, Howard K ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b LAWRENCE LIVERMORE NATIONAL LABORATORY   (United States)

^c Disetronic Medical Systems AG   (Switzerland)

Author keywords

Circular permutation; Cooperativity; Folding; Protein engineering; Stability

Indexed keywords

ASPARTATE AMINOTRANSFERASE; GENE PRODUCT; POLYPEPTIDE; PROTEIN PYRB; SPARFOSIC ACID; UNCLASSIFIED DRUG;

ALLOSTERISM; ALPHA HELIX; ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME ANALYSIS; ESCHERICHIA COLI; GENETIC ENGINEERING; MOLECULAR STABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FOLDING; PROTEIN STABILITY; THERMOSTABILITY;

AMINO ACID SEQUENCE; ASPARTATE CARBAMOYLTRANSFERASE; ASPARTIC ACID; CATALYTIC DOMAIN; ENZYME ACTIVATION; ENZYME STABILITY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HOLOENZYMES; KINETICS; MUTAGENESIS; PHOSPHONOACETIC ACID; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY;

ESCHERICHIA COLI;

EID: 0035100755     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.39001     Document Type: Article

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