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A triple β-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous protein
Human adenoviruses are responsible for respiratory, gastro-enteric and ocular infections and can serve as gene therapy vectors. They form icosahedral particles with 240 copies of the trimeric hexonExpand
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Protein Folding Intermediates and Inclusion Body Formation.
The accumulation of newly synthesized polypeptide chains expressed from cloned genes as non native aggregates has become an important factor in the recovery of such proteins. Studies of both theExpand
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Thermolabile folding intermediates: inclusion body precursors and chaperonin substrates
An unexpected aspect of the expression of cloned genes is the frequent failure of newly synthesized polypeptide chains to reach their native state, accumulating instead as insoluble inclusion bodies.Expand
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Structure of the fiber head of Ad3, a non-CAR-binding serotype of adenovirus.
Adenoviruses of serotype Ad3 (subgenus B) use a still-unknown host cell receptor for viral attachment, whereas viruses from all other known subgenera use the coxsackie and adenovirus receptor (CAR).Expand
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Formation of Highly Stable Chimeric Trimers by Fusion of an Adenovirus Fiber Shaft Fragment with the Foldon Domain of Bacteriophage T4 Fibritin*
The folding of β-structured, fibrous proteins is a largely unexplored area. A class of such proteins is used by viruses as adhesins, and recent studies revealed novel β-structured motifs for them. WeExpand
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Identification of global suppressors for temperature-sensitive folding mutations of the P22 tailspike protein.
Suppressor mutations which alleviate the defects in folding mutants of the P22 gene 9 tailspike protein have recently been isolated (Fane, B. and King, J. (1991) Genetics 127, 263-277). The startingExpand
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Global suppression of protein folding defects and inclusion body formation.
Amino acid substitutions at a site in the center of the bacteriophage protein P22 tailspike polypeptide chain suppress temperature-sensitive folding mutations at many sites throughout the chain.Expand
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Temperature-sensitive mutations and second-site suppressor substitutions affect folding of the P22 tailspike protein in vitro.
One of the central problems in protein folding is how amino acid sequences within polypeptide chains direct polypeptide chain folding and avoid off-pathway aggregation both in intracellularExpand
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Amino acid substitutions influencing intracellular protein folding pathways
Though an increasing variety of chaperonins are emerging as important factors in directing polypeptide chain folding off the ribosome, the primary amino acid sequence remains the major determinant ofExpand
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Design of metal‐binding sites onto self‐assembled peptide fibrils
The ability to develop a rational basis for the binding of inorganic materials to specific binding sites within self‐assembling biological scaffolds has important applications in nanobiotechnology.Expand
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