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Secondary and tertiary structure changes of reconstituted LmrA induced by nucleotide binding or hydrolysis. A fourier transform attenuated total reflection infrared spectroscopy and tryptophan fluorescence quenching analysis.

par Vigano, Catherine ;Margolles, Abelardo;van Veen, Hendrik;Konings, W N;Ruysschaert, Jean Marie
Référence The Journal of biological chemistry, 275, 15, page (10962-10967)
Publication Publié, 2000-04

Article révisé par les pairs

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Titre:	Secondary and tertiary structure changes of reconstituted LmrA induced by nucleotide binding or hydrolysis. A fourier transform attenuated total reflection infrared spectroscopy and tryptophan fluorescence quenching analysis.
Auteur:	Vigano, Catherine; Margolles, Abelardo; van Veen, Hendrik; Konings, W N; Ruysschaert, Jean Marie
Informations sur la publication:	The Journal of biological chemistry, 275, 15, page (10962-10967)
Statut de publication:	Publié, 2000-04
Sujet CREF:	Chimie
MeSH keywords:	ATP-Binding Cassette Transporters -- chemistry
	Bacterial Proteins
	Fluorescence
	Hydrolysis
	Multidrug Resistance-Associated Proteins
	Protein Structure, Secondary
	Protein Structure, Tertiary
	Spectrophotometry, Infrared
	Spectroscopy, Fourier Transform Infrared
	Tryptophan
Note générale:	Journal Article
	Research Support, Non-U.S. Gov't
Langue:	Anglais
Identificateurs:	urn:issn:0021-9258
	info:pmid/10753896