• Citer

The N-terminal domain of the enzyme I is a monomeric well-folded protein with a low conformational stability and residual structure in the unfolded state.

par Romero-Beviar, Manuel;Martínez-Rodríguez, Sergio;Prieto, Jesús;Goormaghtigh, Erik ;Ariz, Usue;Martínez-Chantar, María de la Luz;Gómez, Javier;Neira, José L
Référence Protein engineering, design & selection, 23, 9, page (729-742)
Publication Publié, 2010-09

Article révisé par les pairs

• Accès en ligne
• Détails
• Contenu
• Statistiques

Titre:	The N-terminal domain of the enzyme I is a monomeric well-folded protein with a low conformational stability and residual structure in the unfolded state.
Auteur:	Romero-Beviar, Manuel; Martínez-Rodríguez, Sergio; Prieto, Jesús; Goormaghtigh, Erik; Ariz, Usue; Martínez-Chantar, María de la Luz; Gómez, Javier; Neira, José L
Informations sur la publication:	Protein engineering, design & selection, 23, 9, page (729-742)
Statut de publication:	Publié, 2010-09
Sujet CREF:	Chimie
Mots-clés:	N-terminal domain
	protein stability
	spectroscopy
	structure
	unfolded state
MeSH keywords:	Bacterial Proteins -- chemistry
	Bacterial Proteins -- genetics
	Bacterial Proteins -- metabolism
	Circular Dichroism
	Enzyme Stability
	Escherichia coli -- genetics
	Hydrogen-Ion Concentration
	Hydrophobic and Hydrophilic Interactions
	Nuclear Magnetic Resonance, Biomolecular
	Phosphoenolpyruvate Sugar Phosphotransferase System -- chemistry
	Phosphoenolpyruvate Sugar Phosphotransferase System -- genetics
	Phosphoenolpyruvate Sugar Phosphotransferase System -- metabolism
	Phosphotransferases (Nitrogenous Group Acceptor) -- chemistry
	Phosphotransferases (Nitrogenous Group Acceptor) -- genetics
	Phosphotransferases (Nitrogenous Group Acceptor) -- metabolism
	Protein Conformation
	Protein Denaturation
	Protein Folding
	Recombinant Proteins -- chemistry
	Recombinant Proteins -- genetics
	Recombinant Proteins -- metabolism
	Spectroscopy, Fourier Transform Infrared
	Streptomyces coelicolor -- enzymology
	Streptomyces coelicolor -- genetics
	Thermodynamics
Note générale:	Journal Article
	Research Support, Non-U.S. Gov't
	SCOPUS: ar.j
Langue:	Anglais
Identificateurs:	urn:issn:1741-0126
	info:doi/10.1093/protein/gzq045
	info:pii/gzq045
	info:scp/77956013701
	info:pmid/20630900