Directed evolution of highly homologous proteins with different folds by phage display: Implications for the protein folding code

Biochemistry

Volumn 44, Issue 43, 2005, Pages 14045-14054

  Alexander, Patrick A ^a   Rozak, David A ^a   Orban, John ^a   Bryan, Philip N ^a  

^a UNIVERSITY OF MARYLAND BIOTECHNOLOGY INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIOPHAGES; CHEMICAL BONDS; MUTAGENESIS; NUCLEAR MAGNETIC RESONANCE; STRUCTURE (COMPOSITION); THERMODYNAMIC PROPERTIES;

HETEROMORPHIC PROTEINS; PHAGE DISPLAY; STAPHYLOCOCCAL PROTEIN; TERTIARY STRUCTURES;

PROTEINS;

IMMUNOGLOBULIN G; MUTANT PROTEIN; PROTEIN G; STAPHYLOCOCCUS PROTEIN A;

ALPHA CHAIN; AMINO ACID SEQUENCE; ARTICLE; BETA CHAIN; BINDING AFFINITY; EVOLUTION; MOLECULAR SIZE; MUTAGENESIS; NONHUMAN; PHAGE DISPLAY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; THERMODYNAMICS;

BACTERIAL PROTEINS; BINDING SITES; IMMUNOGLOBULIN G; MAGNETIC RESONANCE SPECTROSCOPY; MUTAGENESIS, SITE-DIRECTED; PEPTIDE LIBRARY; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; STAPHYLOCOCCAL PROTEIN A; THERMODYNAMICS;

HETEROMORPHA; STAPHYLOCOCCUS;

EID: 27444434259     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051231r     Document Type: Article

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