N‐Terminal segment of potato virus X coat protein subunits is glycosylated and mediates formation of a bound water shell on the virion surface

The primary structures of N‐terminal 19‐mer peptides, released by limited trypsin treatment of coat protein (CP) subunits in intact virions of three potato virus X (PVX) isolates, were analyzed. Two wild‐type PVX strains, Russian (Ru) and British (UK3), were used and also the ST mutant of UK3 in whi...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	European journal of biochemistry 2004-08, Vol.271 (15), p.3136-3145
Hauptverfasser:	Baratova, Lyudmila A., Fedorova, Nataliya V., Dobrov, Eugenie N., Lukashina, Elena V., Kharlanov, Andrey N., Nasonov, Vitaly V., Serebryakova, Marina V., Kozlovsky, Stanislav V., Zayakina, Olga V., Rodionova, Nina P.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence bound water Capsid Proteins - chemistry Capsid Proteins - genetics Capsid Proteins - metabolism Carbohydrate Metabolism Carbohydrates - analysis Carbohydrates - chemistry Chromatography, High Pressure Liquid coat protein Electrophoresis, Polyacrylamide Gel Fourier transform infrared spectroscopy Glycosylation Hydrolysis Molecular Sequence Data Mutation - genetics Peptide Fragments - chemistry Peptide Fragments - metabolism Potato virus X Potexvirus - chemistry Potexvirus - metabolism Protein Subunits - chemistry Protein Subunits - genetics Protein Subunits - metabolism Sequence Alignment Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Spectroscopy, Fourier Transform Infrared Trypsin - metabolism Virion - chemistry Virion - metabolism Water - chemistry
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!