FAP mutations destabilize transthyretin facilitating conformational changes required for amyloid formation.

doi:10.1002/9780470514924.ch14

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Article

FAP mutations destabilize transthyretin facilitating conformational changes required for amyloid formation.

Ciba Foundation symposium - 1 Jan 1996

Colon W, Lai Z, McCutchen S L, Miroy G J, Strang C, Kelly J W

Abstract excerpt

Functional transthyretin (TTR) can be transformed into amyloid by partial acid denaturation yielding a monomeric amyloidogenic intermediate which self-associates. The amyloidogenic intermediate has substantial beta-sheet structure with non-native but defined tertiary structure. pH-dependent prote...

Topics

Amyloid
Amyloidosis
Humans
Models, Molecular
Mutation
Prealbumin
Protein Conformation
Protein Folding

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