Using FlAsH To Probe Conformational Changes in a Large HEAT Repeat Protein

We have investigated the use of FlAsH, a small fluorogenic molecule that binds to tetracysteine motifs, to probe folding of the 15‐HEAT repeat protein PR65A. PR65A is one of a special class of modular non‐globular proteins known as tandem repeat proteins, which are composed of small structural motif...

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Veröffentlicht in:	Chembiochem : a European journal of chemical biology 2012-05, Vol.13 (8), p.1199-1205
Hauptverfasser:	Tsytlonok, Maksym, Itzhaki, Laura S.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Binding Sites conformation analysis Cysteine - chemistry Cysteine - metabolism FlAsH Fluorescent Dyes - chemistry Nuclear Proteins - chemistry Nuclear Proteins - metabolism PR65A Protein Conformation protein folding Spectrometry, Fluorescence - methods Tandem Repeat Sequences tetracysteine
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