Prospecting the Proteome: Identification of Naturally Occurring Binding Motifs for Biarsenical Probes

Don't be too rigid. Fluorescent biarsenical probes function by binding to peptide tags genetically engineered into a protein under study. We have found an improved, less rigid peptide tag to bind FlAsH and other xanthene‐based biarsenicals.

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Bibliographische Detailangaben
Veröffentlicht in:	Chembiochem : a European journal of chemical biology 2007-11, Vol.8 (16), p.1937-1940
Hauptverfasser:	Wang, Ting, Yan, Ping, Squier, Thomas C, Mayer, M. Uljana
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Motifs Amino Acid Sequence arsenic Arsenicals - chemistry BASIC BIOLOGICAL SCIENCES Binding Sites bioorganic chemistry Cysteine - chemistry Escherichia coli - chemistry Fluorescent Dyes - chemistry fluorescent probes fluroescent probes Models, Molecular Molecular Sequence Data PEPTIDES Peptides - chemistry photoaffinity labeling photoaffinity labels PROBES PROSPECTING PROTEINS Proteome Shewanella - chemistry
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Beschreibung
Zusammenfassung:	Don't be too rigid. Fluorescent biarsenical probes function by binding to peptide tags genetically engineered into a protein under study. We have found an improved, less rigid peptide tag to bind FlAsH and other xanthene‐based biarsenicals.
ISSN:	1439-4227 1439-7633
DOI:	10.1002/cbic.200700209