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Protein Folding01:22

Protein Folding

128.8K
Overview
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Protein Folding01:25

Protein Folding

11.9K
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...
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Protein Organization01:13

Protein Organization

159.3K
Overview
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Protein Organization01:24

Protein Organization

9.8K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

20.2K
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...
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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Updated: Feb 26, 2026

Microfluidic Mixers for Studying Protein Folding
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Microfluidic Mixers for Studying Protein Folding

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タンパク質フォールディングにおける鎖凝縮と構造形成の間の結合を調節する中間的ヘテロジニティ

Anushka Kaushik1, Jayant B Udgaonkar1

  • 1Department of Biology, Indian Institute of Science Education and Research, Pune, India.

Protein science : a publication of the Protein Society
|February 24, 2026
PubMed
まとめ

タンパク質フォールディングは、鎖凝縮と構造形成を伴います。この研究は、背骨の剛性によって影響される中間状態のヘテロジニティが、タンパク質フォールディング中の凝縮と構造形成の独立した制御を可能にすることを示しています。

キーワード:
背骨の剛性鎖凝縮フォールディング中間体最大エントロピー法タンパク質フォールディング構造的ヘテロジニティ時間分解FRET

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