Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
Article Abstract:
Characterization of the fold of the core protein of hepatitis B virus was performed using electron cryomicroscopy. The complete fold and resulting shell architecture of the polypeptide chain, unlike the standard beta-sheet jelly-roll packings found in previously solved viral capsid proteins, is largely alpha-helical. The dimer clustering of subunits produces spikes on the surface of the icosahedral shell, which consists of radial bundles of four long alpha-helices.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Recombination of protein domains facilitated by co-translational folding in eukaryotes
Article Abstract:
The successful folding into modular polypeptides of pre-existing protein domains is significant in the evolution of complex genomes. The hypothesis that sequential domain folding during ribosome synthesis reduces errors in folding for complex proteins is tested. The results show that rapid and efficient folding of proteins in the eukaryotic system, depends on squential domain folding during synthesis.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
Article Abstract:
A process involving cyclic amplification of protein misfolding that permits a rapid conversion of large excess PrP(super C) into a protease-resistant, PrP(super Sc)-like form when very small quantities of PrP(super Sc) template are present is discussed. This is a strategy for detecting low quantities of PrP(super Sc).
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2001
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