関連する実験動画

Updated: Jun 26, 2026

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
10:09

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

タンパク質の折り畳み速度と安定性:サイズを超えてどのくらいあるのか?

David De Sancho1, Urmi Doshi, Victor Muñoz

  • 1Centro de Investigaciones Biológicas, Spanish National Research Council (CSIC), Ramiro de Maeztu 9, Madrid 28040, Spain.

Journal of the American Chemical Society
|January 28, 2009
PubMed
まとめ

タンパク質のサイズは,配列や構造よりも,折り畳み率と安定性の主要な要因です. タンパク質エネルギーにおける小さな変化が折りたたみに影響を及ぼしますが,自然タンパク質は驚くべき一貫性を示しています.

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Microfluidic Mixers for Studying Protein Folding

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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

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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.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

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Protein Folding01:22

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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...
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...
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...