Predicted fold for the ABri amyloid subunit: A model for amyloidogenesis in Familial British Dementia

D. Mahadevan; T. Chattopadhyay; R. A. Palmer; R. O'Brien; J. W. Saldanha

doi:10.2174/0929866013409472

Predicted fold for the ABri amyloid subunit: A model for amyloidogenesis in Familial British Dementia

D. Mahadevan, T. Chattopadhyay, R. A. Palmer, R. O'Brien, J. W. Saldanha

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

Abstract

ABri is a 34 residue polypeptide that forms amyloid fibrils in Familial British Dementia (FBD). A PSI-Blast search, 3 different fold recognition programs and 3D model-building indicated that it has 3 β-strands forming an antiparallel β-sheet and a small C-terminal α-helix. In order to validate the prediction, the region coding the ABri polypeptide was cloned, expressed and purified from E. Coli. Circular Dichroism (CD) spectroscopy of ABri in aqueous solution shows it to have a predominantly β-sheet structure with a small α-helical component.

Original language	English (US)
Pages (from-to)	171-178
Number of pages	8
Journal	Protein and Peptide Letters
Volume	8
Issue number	3
DOIs	https://doi.org/10.2174/0929866013409472
State	Published - 2001
Externally published	Yes

ASJC Scopus subject areas

Structural Biology
Biochemistry

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abstract = "ABri is a 34 residue polypeptide that forms amyloid fibrils in Familial British Dementia (FBD). A PSI-Blast search, 3 different fold recognition programs and 3D model-building indicated that it has 3 β-strands forming an antiparallel β-sheet and a small C-terminal α-helix. In order to validate the prediction, the region coding the ABri polypeptide was cloned, expressed and purified from E. Coli. Circular Dichroism (CD) spectroscopy of ABri in aqueous solution shows it to have a predominantly β-sheet structure with a small α-helical component.",

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AU - Chattopadhyay, T.

AU - Palmer, R. A.

AU - O'Brien, R.

AU - Saldanha, J. W.

PY - 2001

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AB - ABri is a 34 residue polypeptide that forms amyloid fibrils in Familial British Dementia (FBD). A PSI-Blast search, 3 different fold recognition programs and 3D model-building indicated that it has 3 β-strands forming an antiparallel β-sheet and a small C-terminal α-helix. In order to validate the prediction, the region coding the ABri polypeptide was cloned, expressed and purified from E. Coli. Circular Dichroism (CD) spectroscopy of ABri in aqueous solution shows it to have a predominantly β-sheet structure with a small α-helical component.

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Predicted fold for the ABri amyloid subunit: A model for amyloidogenesis in Familial British Dementia

Abstract

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