関連する実験動画

Updated: Jun 10, 2025

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

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原生質量スペクトロメトリーを用いたタンパク質組成の経路と熱力学の解読

Duong T Bui1, Elena N Kitova1, Pavel I Kitov1

  • 1Department of Chemistry, University of Alberta, Edmonton, Alberta, Canada T6G 2G2.

Journal of the American Chemical Society
|October 10, 2024
PubMed
まとめ

複雑な反応におけるタンパク質組立熱力学を定量化する新しいゆっくり混合モードネイティブ質量スペクトロメトリ (SLOMO-nMS) 方法. この技術は新しい経路と結合 afinitiesを明らかにし,タンパク質の小分子化と病気の理解を進める.

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Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
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Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
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Protein Folding

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.
Protein Structure Is Critical to Its Biological Function
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