TAILIEUCHUNG - Báo cáo khoa học: Amyloid structure – one but not the same: the many levels of fibrillar polymorphism

Many proteins and peptides can form amyloid-like structures bothin vivo andin vitro. Although strikingly similar fibrillar structures can be observed across a variety of amino acid sequences, the fibrils formed often exhibit a stunning wealth of polymorphisms at the level of electron or atomic force microscopy. | ỊFEBS Journal MINIREVIEW Amyloid structure - one but not the same the many levels of fibrillar polymorphism Jesper S. Pedersen1 Christian B. Andersen2 3 and Daniel E. Otzen4 1 Department of Biochemistry Molecular Biology and CellBiology Rice Institute for BiomedicalResearch Northwestern University Evanston IL USA 2 Protein Structure and Biophysics Novo Nordisk A S Malov Denmark 3 Institute of Biophysics NationalResearch Council CNR Palermo Italy 4 Department of Molecular Biology Center for Insoluble Protein Structures Interdisciplinary Nanoscience Centre University of Aarhus Denmark Keywords aggregation amyloid fibrillar polymorphism glucagon mechanism protein folding Correspondence J. S. Pedersen Department of Biochemistry Molecular Biology and Cell Biology Rice Institute for Biomedical Research Northwestern University 2205 Tech Drive Hogan 2-100 Evanston IL 60208 USA Tel 1 847 881 6617 E-mail jsp@ D. Otzen Department of Molecular Biology Center for Insoluble Protein Structures Interdisciplinary Nanoscience Centre University of Aarhus Gustav Wieds Vej10 DK-8000 Aarhus C Denmark Fax 45 8612 3178 Tel 45 8942 5046 E-mail dao@ Received 16 April2010 revised 2 September 2010 accepted 17 September 2010 doi Many proteins and peptides can form amyloid-like structures both in vivo and in vitro. Although strikingly similar fibrillar structures can be observed across a variety of amino acid sequences the fibrils formed often exhibit a stunning wealth of polymorphisms at the level of electron or atomic force microscopy. This appears to violate the Anfinsen principle seen for globular proteins where each protein sequence codes for just one well-defined fold. To a large extent polymorphism reflects variable packing of a single protofilament structure in the mature fibrils. However we and others have recently demonstrated that polymorphism can also reflect real structural differences in the molecular packing of the polypeptide .

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