A natural motif approach to protein design: A synthetic leucine zipper peptide mimics the biological function of the platelet factor 4 protein

FEBS Letters

Volumn 409, Issue 2, 1997, Pages 183-187

  Butcher, Daniel J ^a   Kowalska, M Anna ^b   Li, Song ^a   Luo, Zhaowen ^a   Shan, Simei ^a   Lu, Zhixian ^a   Niewiarowski, Stefan ^b   Huang, Ziwei ^a  

^a THOMAS JEFFERSON UNIVERSITY   (United States)

^b TEMPLE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Circular dichroism; Heparin binding; Leucine zipper; Platelet factor 4; Protein design

Indexed keywords

HEPARIN; PEPTIDE; THROMBOCYTE FACTOR 4;

ARTICLE; BINDING AFFINITY; CIRCULAR DICHROISM; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN BINDING;

AMINO ACID SEQUENCE; ANTIGENS, CD; DNA-BINDING PROTEINS; FUNGAL PROTEINS; HEPARIN; INTERLEUKIN-8; LEUCINE ZIPPERS; MOLECULAR SEQUENCE DATA; NEUTROPHIL ACTIVATION; PEPTIDES; PLATELET FACTOR 4; PROTEIN ENGINEERING; PROTEIN KINASES; RECEPTORS, INTERLEUKIN; RECEPTORS, INTERLEUKIN-8A; SACCHAROMYCES CEREVISIAE PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0030956782     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(97)00504-8     Document Type: Article

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