High-affinity recognition of lanthanide(iii) chelate complexes by a reprogrammed human lipocalin 2

Journal of the American Chemical Society

Volumn 131, Issue 10, 2009, Pages 3565-3576

  Kim, Hyun Jin ^a   Eichinger, Andreas ^a   Skerra, Arne ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID RESIDUES; BINDING ACTIVITIES; CHELATE COMPLEX; DISSOCIATION CONSTANT; E. COLI; ENTEROBACTIN; FUNCTIONALIZED; FUSION PARTNERS; HIGH YIELD; IN-VITRO; LANTHANIDES; LIPOCALIN; LIPOCALIN 2; MEDICAL DIAGNOSTICS; METAL-CHELATE COMPLEX; MODE OF BINDING; NATURAL LIGANDS; NEUTROPHIL GELATINASE-ASSOCIATED LIPOCALIN; PHAGE DISPLAY; POLYPEPTIDE CHAIN; RANDOM MUTAGENESIS; SIDE CHAINS; SIDEROPHORES; SMALL SIZE; STRUCTURAL STUDIES; SURFACE PLASMONS; X-RAY CRYSTALLOGRAPHIC ANALYSIS;

AMINATION; AMINES; AMINO ACIDS; ANTIBODIES; BACTERIOLOGY; CHELATION; DISSOCIATION; DYES; ESCHERICHIA COLI; GADOLINIUM; ISOTOPES; METAL IONS; MUTAGENESIS; ORGANIC ACIDS; RADIOISOTOPES; SURFACE PLASMON RESONANCE; TRACE ANALYSIS;

LIGANDS;

AMINO ACID; ENTEROCHELIN; GADOLINIUM; IRON; ISOTOPE; LANTHANIDE; LUTETIUM; METAL ION; NEUTROPHIL GELATINASE ASSOCIATED LIPOCALIN; PENTETIC ACID; TERBIUM; YTTRIUM; ACUTE PHASE PROTEIN; CHELATING AGENT; LCN2 PROTEIN, HUMAN; LIGAND; LIPOCALIN; ONCOPROTEIN; PRIMER DNA;

ARTICLE; BACTERIOPHAGE; BINDING AFFINITY; CONTROLLED STUDY; DISSOCIATION CONSTANT; ENZYME LINKED IMMUNOSORBENT ASSAY; ESCHERICHIA COLI; GENE LIBRARY; GENETIC VARIABILITY; IN VITRO STUDY; MUTAGENESIS; NONHUMAN; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN PROCESSING; SURFACE PLASMON RESONANCE; X RAY CRYSTALLOGRAPHY; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; METABOLISM; NUCLEOTIDE SEQUENCE; POLYMERASE CHAIN REACTION;

ACUTE-PHASE PROTEINS; BASE SEQUENCE; CHELATING AGENTS; CRYSTALLOGRAPHY, X-RAY; DNA PRIMERS; HUMANS; LANTHANOID SERIES ELEMENTS; LIGANDS; LIPOCALINS; MODELS, MOLECULAR; POLYMERASE CHAIN REACTION; PROTO-ONCOGENE PROTEINS;

EID: 67749142080     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja806857r     Document Type: Article

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