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Updated: Jul 10, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
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Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

BLUFドメインにおける超高速構造ダイナミクス:AppAとその変異体の一時的な赤外線スペクトル検査

Allison L Stelling1, Kate L Ronayne, Jérôme Nappa

  • 1Department of Chemistry, Stony Brook University, Stony Brook, New York 11794-3400, USA.

Journal of the American Chemical Society
|November 23, 2007
PubMed
まとめ

超高速スペクトロスコピーは,BLUFドメインタンパク質の初期構造変化を,光活性化時に明らかにします. 染色体相互作用を含むこれらのダイナミクスは,タンパク質の光周期とシグナル伝達に不可欠です.

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Submillisecond Conformational Changes in Proteins Resolved by Photothermal Beam Deflection

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Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...