Exploring the folding pathways of annexin I, a multidomain protein. I. non-native structures stabilize the partially folded state of the isolated domain 2 of annexin I

Proteins of the annexin family constitute very attractive models because of their four ∼70 residue domains, D1 to D4, exhibiting an identical topology comprising five helix segments with only a limited sequence homology of approximately 30%. We focus on the isolated D2 domain, which is only partiall...

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Veröffentlicht in:	Journal of molecular biology 1998-06, Vol.279 (5), p.1163-1175
Hauptverfasser:	Cordier-Ochsenbein, Françoise, Guerois, Raphaël, Baleux, Françoise, Huynh-Dinh, Tam, Lirsac, Pierre-Noël, Russo-Marie, Françoise, Neumann, Jean-Michel, Sanson, Alain
Format:	Artikel
Sprache:	eng
Schlagworte:	annexin Annexin A1 - chemistry Escherichia coli - chemistry Magnetic Resonance Spectroscopy Micelles NMR non-native structures Peptide Fragments - chemistry Polytetrafluoroethylene - pharmacology Protein Conformation - drug effects Protein Folding stability
Online-Zugang:	Volltext
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