Fluorescence Characterization of the Hydrophobic Pocket of Cyclophilin B

Human cyclophilin B is a monomeric protein that contains two tryptophan residues, Trp104 and 128. Trp128-residue belongs to the binding site of cyclosporin A and is the homologous of Trp 121 in CyPA, while Trp104 residue belongs to the hydrophobic pocket. In the present work, we studied the dynamics...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Journal of fluorescence 2008, Vol.18 (1), p.75-85
Hauptverfasser:	Albani, J. R., Carpentier, M., Lansiaux, C.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical Chemistry Binding Sites Biochemistry Biological and Medical Physics Biomedical and Life Sciences Biomedicine Biophysics Biotechnology Cyclophilins - chemistry Cyclophilins - genetics Cyclophilins - metabolism Fluorescence Fluorescence Polarization Humans Hydrophobic and Hydrophilic Interactions Mutation - genetics Naphthalenesulfonates - chemistry Naphthalenesulfonates - metabolism Original Paper Peptidylprolyl Isomerase - chemistry Peptidylprolyl Isomerase - genetics Peptidylprolyl Isomerase - metabolism Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Spectrometry, Fluorescence Tryptophan - chemistry
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!