Buch, Englisch, 528 Seiten, Format (B × H): 163 mm x 239 mm, Gewicht: 885 g
Structural Disorder in Viral Proteins
Buch, Englisch, 528 Seiten, Format (B × H): 163 mm x 239 mm, Gewicht: 885 g
ISBN: 978-0-470-61831-8
Verlag: Wiley
Autoren/Hrsg.
Fachgebiete
Weitere Infos & Material
Preface.
1. Do viral proteins possess unique features? (Vladimir Uversky).
2. Functional role of structural disorder in capsid proteins (Lars Liljas).
3. Structural disorder within the nucleoproteins and phosphoproteins of measles, Nipah and Hendra viruses (Johnny Habchi and Sonia Longhi).
4. Structural disorder within the Sendai virus nucleoprotein and phosphoprotein (Rob Ruigrok and Martin Blackledge).
5. Structural disorder in Rhabdoviridae phosphoproteins (Marc Jamin).
6. Structural disorder in matrix proteins from HiV-related viruses (Vladimir Uversky and Keith Dunker).
7. Structural disorder in proteins from influenza virus (Vladmir Uversky and Keith Dunker).
8. Structural disorder in the HIV-1 Vif protein and oilgomerization-dependent gain of structure (Assaf Friedler).
9. Order from Disorder: Structure, Function and Dynamics of the HIV-1 Transactivator of Transcription (Joe D. O'Neil).
10. Intrinsically disordered protein domains of the non structural proteins of Sesbania mosaic virus and their functional role (Handanahal S. Savithri).
11. Intrinsic disorder in genome-linked viral proteins VPgs of potyviruses (Jadwiga Chroboczek, Eugénie Hébrard, Kristiina Mäkinen, Thierry Michon and Kimmo Rantalainen).
12. Intrinsic disorder in HPV 16 E7 protein (Gonzalo de Prat-Gay).
13. The Semiliki forest virus serine protease is disordered and yet displays catalytic activity (Manuel Morillas).
14. Intrinsic disorder in the core proteins of Flaviviridae (Jean-Luc Darlix).
15. Domains 2 and 3 of non-structural protein 5A (NS5A) of hepatitis C virus is natively unfolded (Ho Sup Yoon).
16. Intrinsic disorder within phage " N protein and interaction with the E. coli NusA protein (Kristian Schweimer).
17. The N-terminal extension region of Hordeivirus movement TGB1 protein consists of two domains with different content of disordered structure (V.V. Makarov, M.E. Tailansky, E.N. Dobrov, N.O. Kalinina).