Hydrogen/deuterium exchange mass spectrometry analysis of protein aggregates (Q79258627)

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20 December 2019

title

Hydrogen/deuterium exchange mass spectrometry analysis of protein aggregates (English)

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20 December 2019

2

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20 December 2019

author name string

Indu Kheterpal

series ordinal

1

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20 December 2019

Ronald Wetzel

series ordinal

3

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20 December 2019

publication date

1 January 2006

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20 December 2019

published in

Methods in Enzymology

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20 December 2019

volume

413

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20 December 2019

page(s)

140-166

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Enhanced prediction accuracy of protein secondary structure using hydrogen exchange Fourier transform infrared spectroscopy

20 December 2019

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Protein analysis by hydrogen exchange mass spectrometry

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Mapping the core of the beta(2)-microglobulin amyloid fibril by H/D exchange

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Hydrogen/deuterium exchange and aggregation of a polyvaline and a polyleucine alpha-helix investigated by matrix-assisted laser desorption ionization mass spectrometry

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Intramolecular migration of amide hydrogens in protonated peptides upon collisional activation

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Abeta protofibrils possess a stable core structure resistant to hydrogen exchange

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Enhanced correction methods for hydrogen exchange-mass spectrometric studies of amyloid fibrils

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Abeta amyloid fibrils possess a core structure highly resistant to hydrogen exchange

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Hydrogen exchange studies on Alzheimer's amyloid-beta peptides by mass spectrometry using matrix-assisted laser desorption/ionization and electrospray ionization

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NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126.

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Site-specific amide hydrogen exchange in melittin probed by electron capture dissociation Fourier transform ion cyclotron resonance mass spectrometry.

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Mixtures of wild-type and a pathogenic (E22G) form of Abeta40 in vitro accumulate protofibrils, including amyloid pores.

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[18] Quantification of β-sheet amyloid fibril structures with thioflavin T

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Conformational transition occurring upon amyloid aggregation of the HET-s prion protein of Podospora anserina analyzed by hydrogen/deuterium exchange and mass spectrometry

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Probing Solvent Accessibility of Transthyretin Amyloid by Solution NMR Spectroscopy

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Is the slow exchange core the protein folding core?

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Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor

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Core and heterogeneity of beta2-microglobulin amyloid fibrils as revealed by H/D exchange

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Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation

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7 January 2021

10.1016/S0076-6879(06)13008-6

Identifiers

DOI

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20 December 2019

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