関連する実験動画

Updated: Jul 16, 2026

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
10:50

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

Published on: September 15, 2010

螺旋状タンパク質の折りたたみ運動を解釈する

Y Zhou1, M Karplus

  • 1Department of Chemistry & Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA.

Nature
|October 12, 1999
PubMed
まとめ

タンパク質の折り畳みメカニズムを理解することは極めて重要です. この研究は,異なるネイティブと非ネイティブの接触強度が,拡散衝突から同時崩壊と再編成に至るまで,タンパク質の折り畳み経路をどのように変化させるかを明らかにしています.

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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

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Microfluidic Mixers for Studying Protein Folding

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Protein Organization01:13

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Protein Folding

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Protein Folding01:22

Protein Folding

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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...
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...
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...