A Study of the Α-Helical Intermediate Preceding the Aggregation of the Amino-Terminal Fragment of the Β Amyloid Peptide (Aβ1–28)

Journal of Physical Chemistry B- United States

doi 10.1021/jp2050993

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Date

November 10, 2011

Authors

Ana V. Rojas

Adam Liwo

Harold A. Scheraga

Publisher

American Chemical Society (ACS)

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A Study of the Α-Helical Intermediate Preceding the Aggregation of the Amino-Terminal Fragment of the Β Amyloid Peptide (Aβ1–28)

Journal of Physical Chemistry B- United States

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

The Metalloprotease Meprin Β Generates Amino Terminal-Truncated Amyloid Β Peptide Species

Generation of the Β-Amyloid Peptide and the Amyloid Precursor Protein C-Terminal Fragment Γ Are Potentiated by FE65L1

The Norepinephrine Inhibits Alzheimer's Amyloid-Β Peptide Aggregation by Binding to the C-Terminal Hydrophobic Region

The Β Amyloid Peptide Can Act as a Modular Aggregation Domain

The A673T Mutation in the Amyloid Precursor Protein Reduces the Production of Β-Amyloid Protein From Its Β-Carboxyl Terminal Fragment in Cells

Conformational Studies of the Α-Helical 28-43 Fragment of the B3 Domain of the Immunoglobulin Binding Protein G fromStreptococcus

L17a/F19a Substitutions Augment the Α-Helicity of Β-Amyloid Peptide Discordant Segment

Molecular Dynamics Simulation on the Effect of Transition Metal Binding to the N-Terminal Fragment of Amyloid-Β

Erratum to “Regulation of Aggregation of Self-Associated Peptides, Including N-Terminal Fragments of the Alzheimer’s Β-Amyloid Peptide, by Nitro Derivatives of Azoloazine”