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Solution structure and stability of the full-length excisionase from bacteriophage HK022

✍ Scribed by Vladimir V. Rogov; Christian Lücke; Lucia Muresanu; Hans Wienk; Ioana Kleinhaus; Karla Werner; Frank Löhr; Primož Pristovšek; Heinz Rüterjans


Book ID
110914890
Publisher
John Wiley and Sons
Year
2003
Tongue
English
Weight
506 KB
Volume
270
Category
Article
ISSN
1432-1327

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The aggregation and structural properties of the synthetic C-terminal half [Ala 330 , Ala 350 )270-373; 104-mer)] polypeptide from HIV-1 p24gag were studied. In concentrated solutions the synthetic polypeptide aggregated to tetramers which, upon dilution, gave a mixture of monomeric and dimeric spec