The full amino acid repertoire is superior to serine/tyrosine for selection of high affinity immunoglobulin G binders from the fibronectin scaffold

Protein Engineering, Design and Selection

Volumn 23, Issue 4, 2010, Pages 211-219

  Hackel, Benjamin J ^a   Wittrup, K Dane ^a,b  

^a Massachusetts Institute of Technology Cambridge   (United States)

^b MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

fibronectin type III domain; Fn3; immunoglobulin G; protein engineering; synthetic library

Indexed keywords

FIBRONECTIN TYPE III; FN3; IMMUNOGLOBULIN G; PROTEIN ENGINEERING; SYNTHETIC LIBRARY;

AMINO ACIDS; BIOCHEMICAL ENGINEERING; FLOW CYTOMETRY; GENETIC ENGINEERING; LIBRARIES; MOLECULAR BIOLOGY; MOLECULAR RECOGNITION; ORGANIC ACIDS; PROTEINS;

BINDERS;

AMINO ACID; FIBRONECTIN; IMMUNOGLOBULIN G; SERINE; TYROSINE; PEPTIDE LIBRARY;

ANIMAL EXPERIMENT; ARTICLE; BINDING AFFINITY; CLONING; COMBINATORIAL LIBRARY; CONTROLLED STUDY; FLOW CYTOMETRY; GOAT; MATURATION; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ENGINEERING; RABBIT; SEQUENCE ANALYSIS; AMINO ACID SEQUENCE; CHEMISTRY; GENETICS; HUMAN; METABOLISM;

CAPRA HIRCUS; ORYCTOLAGUS CUNICULUS;

AMINO ACID SEQUENCE; FIBRONECTINS; HUMANS; IMMUNOGLOBULIN G; PEPTIDE LIBRARY; PROTEIN ENGINEERING; SERINE; TYROSINE;

EID: 77954626231     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzp083     Document Type: Article

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