Structural and Dynamical Properties of a Partially Unfolded Fe4S4 Protein:  Role of the Cofactor in Protein Folding

Heteronuclear multidimensional NMR spectroscopy was used to investigate in detail the structural and dynamical properties of a partially unfolded intermediate of the reduced high-potential iron−sulfur protein (HiPIP) from Chromatium vinosum present in 4 M guanidinium chloride solution. After an exte...

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Veröffentlicht in:	Biochemistry (Easton) 1999-04, Vol.38 (15), p.4669-4680
Hauptverfasser:	Bentrop, Detlef, Bertini, Ivano, Iacoviello, Rita, Luchinat, Claudio, Niikura, Yohei, Piccioli, Mario, Presenti, Chiara, Rosato, Antonio
Format:	Artikel
Sprache:	eng
Schlagworte:	Iron-Sulfur Proteins - chemistry Magnetic Resonance Spectroscopy Models, Molecular Protein Conformation Protein Folding Recombinant Proteins - chemistry
Online-Zugang:	Volltext
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