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関連する概念動画

Protein Folding01:22

Protein Folding

Overview
Peptide Bonds02:43

Peptide Bonds

A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
Protein Folding01:22

Protein Folding

Overview
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
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-Protein Interfaces02:04

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

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関連する実験動画

Updated: May 12, 2026

Measurement of Force-Sensitive Protein Dynamics in Living Cells Using a Combination of Fluorescent Techniques
08:28

Measurement of Force-Sensitive Protein Dynamics in Living Cells Using a Combination of Fluorescent Techniques

Published on: November 2, 2018

トランジションの過程で,タンパク質は一時的な結合をします.

David D Boehr1

  • 1Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA.

Cell
|December 17, 2009
PubMed
まとめ
この要約は機械生成です。

暫定的な水素結合は,タンパク質の構成の変化の鍵である. この研究は,窒素調節タンパク質NtrCCにおける彼らの重要な役割を明らかにしています.

科学分野:

  • バイオケミストリー バイオケミストリー
  • 分子生物学は分子生物学である.
  • 構造生物学 構造生物学とは

背景:

  • タンパク質は,機能を遂行するために,形状の変化を経験します.
  • 窒素調節タンパク質NtrCは,ネイティブ状態と活性状態の間の移行をします.

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Utilization of Grafix for the Detection of Transient Interactors of Saccharomyces cerevisiae Spliceosome Subcomplexes

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Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
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Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates

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関連する実験動画

Last Updated: May 12, 2026

Measurement of Force-Sensitive Protein Dynamics in Living Cells Using a Combination of Fluorescent Techniques
08:28

Measurement of Force-Sensitive Protein Dynamics in Living Cells Using a Combination of Fluorescent Techniques

Published on: November 2, 2018

Utilization of Grafix for the Detection of Transient Interactors of Saccharomyces cerevisiae Spliceosome Subcomplexes
05:44

Utilization of Grafix for the Detection of Transient Interactors of Saccharomyces cerevisiae Spliceosome Subcomplexes

Published on: November 9, 2020

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
06:48

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates

Published on: January 5, 2024