Polymer-based protein engineering can rationally tune enzyme activity, pH-dependence, and stability

Biomacromolecules

Volumn 14, Issue 6, 2013, Pages 1919-1926

  Murata, Hironobu ^a   Cummings, Chad S ^a   Koepsel, Richard R ^a   Russell, Alan J ^a  

^a CARNEGIE MELLON UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2-(DIMETHYLAMINO)ETHYL METHACRYLATE; BIOTECHNOLOGY INDUSTRY; INERT POLYMERS; MODEL PROTEINS; PH-DEPENDENCE; PH-RESPONSIVE POLYMER; POLYMER ARCHITECTURE; PROTEIN ENGINEERING;

ATOM TRANSFER RADICAL POLYMERIZATION; BIOCHEMICAL ENGINEERING; ENZYMES; GENETIC ENGINEERING; PROTEINS;

POLYMERS;

CHYMOTRYPSIN; MACROGOL; POLY[2 (DIMETHYLAMINO)ETHYL METHACRYLATE]; POLYMER;

AQUEOUS SOLUTION; ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CONFORMATIONAL TRANSITION; CONJUGATION; COVALENT BOND; ENZYME ACTIVITY; ENZYME REGULATION; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN ENGINEERING; PROTEIN INTERACTION; PROTEIN STABILITY; SOLVENT EFFECT; SURFACE PROPERTY; TEMPERATURE DEPENDENCE;

ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; KINETICS; POLYMERS; PROTEIN ENGINEERING; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; TEMPERATURE;

EID: 84878861673     PISSN: 15257797     EISSN: 15264602     Source Type: Journal    
DOI: 10.1021/bm4002816     Document Type: Article

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