Energetics of Assembling an Artificial Heterodimer with an α/β Motif: Cleaved versus Uncleaved Escherichia coli Thioredoxin

We have studied the folding/binding process between the N- and C-fragments (1−73, 74−108) of oxidized Escherichia coli thioredoxin (Trx) to compare the energetics between the cleaved and uncleaved Trx. Sedimentation equilibrium analysis in 0.1 M potassium phosphate, pH 5.7, shows (i) the strong and...

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Veröffentlicht in:	Biochemistry (Easton) 1999-10, Vol.38 (40), p.13355-13366
Hauptverfasser:	Georgescu, Roxana E, Braswell, Emory H, Zhu, Dan, Tasayco, María Luisa
Format:	Artikel
Sprache:	eng
Schlagworte:	Circular Dichroism Dimerization Escherichia coli Escherichia coli - chemistry Hydrolysis Models, Chemical Nuclear Magnetic Resonance, Biomolecular Peptide Fragments - chemistry Peptide Fragments - isolation & purification Protein Binding Protein Folding Protein Structure, Secondary Spectrometry, Fluorescence Temperature Thermodynamics thioredoxin Thioredoxins - chemistry Ultracentrifugation
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