Lysine acetylation can generate highly charged enzymes with increased resistance toward irreversible inactivation

Protein Science

Volumn 17, Issue 8, 2008, Pages 1446-1455

  Shaw, Bryan F ^a   Schneider, Gregory F ^a   Bilgiçer, Başar ^a   Kaufman, George K ^a   Neveu, John M ^a   Lane, William S ^a   Whitelegge, Julian P ^b   Whitesides, George M ^a  

^a HARVARD UNIVERSITY   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Amylase; Charge ladders; Industrial biotechnology; Protein aggregation; Protein engineering; Sodium dodecyl sulfate; Thermostability

Indexed keywords

AMYLASE; DODECYLTRIMETHYLAMMONIUM BROMIDE; LYSINE; TRITON X 100;

ACETYLATION; ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME CONFORMATION; ENZYME INACTIVATION; ENZYME MODIFICATION; ENZYME STABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ENGINEERING; THERMOSTABILITY;

ACETYLATION; ALPHA-AMYLASES; BACILLUS; BACTERIAL PROTEINS; CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; ELECTROPHORESIS, CAPILLARY; ENZYME STABILITY; LYSINE; OCTOXYNOL; QUATERNARY AMMONIUM COMPOUNDS; SODIUM DODECYL SULFATE; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

BACTERIA (MICROORGANISMS);

EID: 48249157846     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.035154.108     Document Type: Article

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