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Volume 5, Issue 5, Pages 595-600 (May 1997)
Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases Jeffery W Kelly Structure Volume 5, Issue 5, Pages (May 1997) DOI: /S (97)
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Figure 1 Outline of the role that conformational changes play in the conversion of a normally soluble and functional protein into amyloid. Amyloidogenic proteins appear to adopt alternative conformations which have common structural features. Structure 1997 5, DOI: ( /S (97) )
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Figure 2 The pH-dependent denaturation/amyloid fibril formation pathway exhibited by transthyretin (TTR). Structure 1997 5, DOI: ( /S (97) )
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Figure 3 Ligand binding stabilizes the normal fold of the amyloidogenic protein transthyretin (TTR), thus preventing the formation of the alternative conformation which leads to amyloid fibril formation. Structure 1997 5, DOI: ( /S (97) )
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