Bacterial inclusion bodies contain amyloid-like structure

Protein aggregation is a process in which identical proteins self-associate into imperfectly ordered macroscopic entities. Such aggregates are generally classified as amorphous, lacking any long-range order, or highly ordered fibrils. Protein fibrils can be composed of native globular molecules, suc...

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Veröffentlicht in:	PLoS biology 2008-08, Vol.6 (8), p.e195-e195
Hauptverfasser:	Wang, Lei, Maji, Samir K, Sawaya, Michael R, Eisenberg, David, Riek, Roland
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amyloid - metabolism Animals Antigens, Bacterial - genetics Bacteria Bacterial Proteins - genetics Biochemistry Biophysics Biotechnology Bone Morphogenetic Protein 2 Bone Morphogenetic Proteins - genetics Diabetes E coli Enzymes Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli - ultrastructure Experiments Humans Inclusion Bodies - metabolism Inclusion Bodies - ultrastructure Microbiology Molecular Sequence Data Molecular weight Myelin Proteins Myelin-Associated Glycoprotein - genetics Myelin-Oligodendrocyte Glycoprotein Neurological Disorders NMR Nuclear magnetic resonance Parkinson's disease Prokaryotes Protein folding Protein Structure, Secondary Rats Transforming Growth Factor beta - genetics
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