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Related Concept Videos

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...
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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

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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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Measurement of Force-Sensitive Protein Dynamics in Living Cells Using a Combination of Fluorescent Techniques
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Published on: November 2, 2018

During transitions proteins make fleeting bonds.

David D Boehr1

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

Cell
|December 17, 2009
PubMed
Summary
This summary is machine-generated.

Transient hydrogen bonds are key to protein conformational changes. This study reveals their critical role in the nitrogen regulatory protein NtrC

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Proteins undergo conformational changes to perform functions.
  • The nitrogen regulatory protein NtrC transitions between native and active states.

Discussion:

  • Transient hydrogen bonds play a crucial role in protein conformational transitions.
  • These dynamic bonds facilitate the precise shift from NtrC's native to active state.

Key Insights:

  • Identifies transient hydrogen bonds as critical determinants of protein conformational dynamics.
  • Elucidates the mechanism underlying NtrC's functional state transitions.

Outlook:

  • Understanding these mechanisms can inform protein engineering and drug design.
  • Further research into transient hydrogen bond networks in other proteins is warranted.