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Updated: Mar 9, 2026

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
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Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

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単分子原子力顕微鏡で発見されたメタロプロテイン・フェルドキシンの逆転展開と折り畳み

Hai Lei1,2, Yabin Guo2, Xiaodong Hu1

  • 1State Key Laboratory of Precision Measurements Technology and Instruments, School of Precision Instrument and Optoelectronics Engineering, Tianjin University , Tianjin 300072, People's Republic of China.

Journal of the American Chemical Society
|January 12, 2017
PubMed
まとめ

光合成に不可欠な植物フェルドキシンが 逆転可能な展開と再折りについて 研究することができます この単一分子の研究は 鉄と硫黄のクラスターが このプロセスにどのように関与しているかを明らかにし 新しい研究の道を開きます

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Protein Folding01:25

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.
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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.
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