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Updated: Jun 26, 2026

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics
09:18

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

Published on: April 17, 2017

ガス相タウペプチドダイマーにおけるβシート集積の観察

Timothy D Vaden1, Sally A N Gowers, Lavina C Snoek

  • 1Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK. timothy.vaden@chem.ox.ac.uk

Journal of the American Chemical Society
|January 31, 2009
PubMed
まとめ

アルツハイマー病のタウタンパク質の断片は,ベータシートに集積する. これらの構造は,溶媒やタンパク質の影響を必要とせずに,バックボーン水素結合によって駆動され,気相で容易に形成されます.

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Protein Folding01:22

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Protein Folding01:25

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...