Stability and solubility engineering of the EphB4 tyrosine kinase catalytic domain using a rationally designed synthetic library

Protein Engineering, Design and Selection

Volumn 26, Issue 10, 2013, Pages 695-704

  Overman, R C ^a   Green, I ^a   Truman, C M ^a   Read, J A ^a   Embrey, K J ^a   McAlister, M S B ^a   Attwood, T K ^b  

^a ASTRAZENECA   (United Kingdom)

^b UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

combinatorial library; protein engineering; solubility; stability; synthetic genes

Indexed keywords

CATALYTIC DOMAINS; COMBINATORIAL LIBRARY; PROTEIN ENGINEERING; RECEPTOR TYROSINE KINASE; SOLUBLE MATERIALS; STRUCTURAL FACTOR; SYNTHETIC GENES; WILD-TYPE PROTEINS;

AMINO ACIDS; CLONING; CONVERGENCE OF NUMERICAL METHODS; ENZYMES; ESCHERICHIA COLI; GENES; PROTEINS;

SOLUBILITY;

EPHRIN RECEPTOR B4;

AMINO ACID SEQUENCE; ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ENGINEERING; ENZYME STABILITY; ENZYME SYNTHESIS; ESCHERICHIA COLI; IN VITRO STUDY; MOLECULAR LIBRARY; NONHUMAN; PRIORITY JOURNAL; SOLUBILITY; THERMOSTABILITY; WILD TYPE;

COMBINATORIAL LIBRARY; PROTEIN ENGINEERING; SOLUBILITY; STABILITY; SYNTHETIC GENES;

CATALYTIC DOMAIN; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MODELS, MOLECULAR; MUTATION; PEPTIDE LIBRARY; PROTEIN ENGINEERING; PROTEIN STABILITY; RECEPTOR, EPHB4; SOLUBILITY; TEMPERATURE;

EID: 84885000695     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzt032     Document Type: Article

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