Aluminum- and mild steel-binding peptides from phage display

Applied Microbiology and Biotechnology

Volumn 68, Issue 4, 2005, Pages 505-509

  Zuo, Rongjun ^a   Örnek, Dogan ^a,b   Wood, Thomas K ^a  

^a UNIVERSITY OF CONNECTICUT   (United States)

^b GENZYME CORPORATION   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALUMINUM; BACTERIOLOGY; GENETIC ENGINEERING; NUCLEIC ACID SEQUENCES; STEEL;

AMINO ACID RESIDUES; METAL-BINDING PEPTIDES; PHAGE DISPLAY; PHAGE LIBRARIES;

AMINO ACIDS;

ALANYLTHREONYLISOLEUCYLHISTIDYLASPARTYLALANYLPHENYLALANYLTYROSYLSERYL ALANYLPROLYLGLUTAMIC ACID; ALUMINUM; AMINO ACID; ASPARAGINYLASPARAGINYLARGINYLPROLYLGLUTAMYLPROLYLSERYLPROLYLVALYLVALYL PROLYLHISTIDINE; ASPARAGINYLLEUCYLASPARAGINYLPROLYLASPARAGINYLTHREONYLALANYLSERYLALANYL METHIONYLHISTIDYLVALINE; ASPARAGINYLLEUCYLTHREONYLISOLEUCYLALANYLSERYLTYROSYLPROLYLSERYLMETHIONYL VALYLVALINE; GLUTAMINYLMETHIONYLASPARTYLISOLEUCYLSERYLLEUCYLGLYCYLARGINYLTRYPTOPHYL SERYLSERYLMETHIONINE; GLUTAMINYLSERYLHISTIDYLTYROSYLARGINYLHISTIDYLISOLEUCYLSERYLPROLYLALANYL GLUTAMINYLVALINE; HISTIDINE; HYDROXYL GROUP; PEPTIDE; SERINE; SERYLPROLYLLEUCYLASPARTYLGLYCYLLYSYLASPARAGINYLISOLEUCYLPROLYLLEUCYLGLYCYL HISTIDINE; STEEL; THREONINE; THREONYLLEUCYLTRYPTOPHYLSERYLGLUTAMINYLGLYCYLARGINYLSERYLALANYLTYROSYL PROLYLVALINE; TRYPTOPHYLPROLYLALANYLPROLYLALANYLISOLEUCYLTRYPTOPHYLHISTIDYLALANYLPROLYL THREONYLLEUCINE; TYROSYLMETHIONYLLYSYLGLUTAMINYLISOLEUCYLPROLYLALANYLGLYCYLARGINYLTHREONYL ASPARAGINYLPROLINE; TYROSYLSERYLPROLYLASPARTYLPROLYLARGINYLPROLYLTRYPTOPHYLSERYLSERYLARGINYL TYROSINE; UNCLASSIFIED DRUG; VALYLPROLYLSERYLSERYLGLYCYLPROLYLGLUTAMINYLASPARTYLTHREONYLARGINYLTHREONYL THREONINE;

PEPTIDE;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; CORROSION; METAL BINDING; MOLECULAR INTERACTION; NONHUMAN; PHAGE DISPLAY; PROTEIN BINDING; PROTEIN MOTIF; SURFACE PROPERTY;

ALUMINUM; PEPTIDE FRAGMENTS; PEPTIDE LIBRARY; STEEL;

EID: 23644447542     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-005-1922-5     Document Type: Article

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