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Updated: Jun 4, 2026

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
09:37

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

タンパク質の展開における個々の反応経路と,単一のタンパク質内で観察された二硫化結合の減少を比較する

Sergi Garcia-Manyes1, Tzu-Ling Kuo, Julio M Fernández

  • 1Department of Biological Sciences, Columbia University, New York, New York 10027, USA. sergi@biology.columbia.edu

Journal of the American Chemical Society
|February 12, 2011
PubMed
まとめ

この研究は,タンパク質の展開と二酸化硫化物結合の減少が,さまざまなエネルギー障壁を持つ複雑な反応経路を示していることを示しています. フォースクランプスペクトロスコピーは,単分子タンパク質ダイナミクスにおけるこの"静的障害"を定量化します.

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Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae13:52

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Protein Folding01:22

Protein Folding

Overview
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.
Protein Structure Is Critical to Its Biological Function
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Protein Modifications in the RER01:26

Protein Modifications in the RER

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Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
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...
The Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...