Association of the catalytic subunit of aspartate transcarbamoylase with a zinc‐containing polypeptide fragment of the regulatory chain leads to increases in thermal stability

Protein Science

Volumn 3, Issue 6, 1994, Pages 960-966

  Peterson, Cynthia B ^a,b   Zhou, Bin‐Bing ^a   Hsieh, Durwynne ^a,c   Creager, Angela N H ^a,d   Schachman, H K ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF TENNESSEE   (United States)

^c Los Medanos College   (United States)

^d MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

conformational change; differential scanning microcalorimetry; enhanced thermal stability; interchain interaction; zinc domain

Indexed keywords

ASPARTATE CARBAMOYLTRANSFERASE; POLYPEPTIDE; REGULATOR PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME ACTIVE SITE; ENZYME DENATURATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE; THERMOSTABILITY;

ASPARTATE CARBAMOYLTRANSFERASE; BINDING SITES; CALORIMETRY, DIFFERENTIAL SCANNING; CATALYSIS; ENZYME STABILITY; ESCHERICHIA COLI; HEAT; MACROMOLECULAR SYSTEMS; MUTAGENESIS, SITE-DIRECTED; PEPTIDE FRAGMENTS; REGULATORY SEQUENCES, NUCLEIC ACID; STRUCTURE-ACTIVITY RELATIONSHIP; SUPPORT, U.S. GOV'T, NON-P.H.S.; SUPPORT, U.S. GOV'T, P.H.S.; ZINC;

EID: 0028322215     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.5560030611     Document Type: Article

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