Mutational analysis of designed peptides that undergo structural transition from α helix to β sheet and amyloid fibril formation (Q57907586)

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10 November 2019

title

Mutational analysis of designed peptides that undergo structural transition from alpha helix to beta sheet and amyloid fibril formation (English)

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10 November 2019

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3

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10 November 2019

author name string

Y Takahashi

series ordinal

1

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10 November 2019

A Ueno

series ordinal

2

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10 November 2019

publication date

1 September 2000

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10 November 2019

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10 November 2019

volume

8

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10 November 2019

issue

9

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10 November 2019

page(s)

915-925

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Protein aggregation: folding aggregates, inclusion bodies and amyloid

10 November 2019

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Solution structure of amyloid beta-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?

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De novo amyloid proteins from designed combinatorial libraries

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Beta-helical fibrils from a model peptide.

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Responsive gels formed by the spontaneous self-assembly of peptides into polymeric beta-sheet tapes

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Direct conversion of an oligopeptide from a beta-sheet to an alpha-helix: a model for amyloid formation

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Super-Secondary Structure with Amphiphilicβ-Strands Probed by Pyrenylalanine

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Conformational switching in designed peptides: the helix/sheet transition

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Regulation of α/β-folding of a designed peptide by haem binding

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Context-dependent secondary structure formation of a designed protein sequence

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Transmuting alpha helices and beta sheets

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Evolution of a protein fold in vitro

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alpha-->beta transition of beta-lactoglobulin as evidenced by heteronuclear NMR.

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Optimization of Hydrophobic Domains in Peptides that Undergo Transformation from α-Helix to β-Fibril

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Construction of Peptides That Undergo Structural Transition from α-Helix to β-Sheet and Amyloid Fibril Formation by the Introduction of N-Terminal Hydrophobic Amino Acids

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Physical, morphological and functional differences between ph 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Abeta

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Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide

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7 January 2021

Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants

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7 January 2021

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Identifiers

DOI

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10 November 2019

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