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Related Concept Videos

Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Diversity in Cell Signaling Responses01:22

Diversity in Cell Signaling Responses

The physiological function of a cell and cellular communication are outcomes of a range of extrinsic signals, intracellular signaling pathways, and cellular responses. No two cell types express the same repertoire of signaling components. Receptors are highly selective for their cognate ligands, but once activated, they can alter multiple cellular processes such as DNA transcription, protein synthesis, and metabolic activity. 
Graded and Abrupt Responses
Some signaling systems generate...

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Updated: Jun 2, 2026

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

Singlet oxygen's response to protein dynamics.

Rasmus Lybech Jensen1, Jacob Arnbjerg, Henrik Birkedal

  • 1Center for Oxygen Microscopy and Imaging, Chemistry Department, Aarhus University, DK-8000, Århus, Denmark.

Journal of the American Chemical Society
|April 16, 2011
PubMed
Summary

Singlet oxygen removal by proteins is influenced by protein structure. Changes in protein structure, such as denaturation or ligand binding, alter the rate of singlet oxygen quenching, impacting cellular processes.

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Area of Science:

  • Biochemistry
  • Chemical Biology
  • Cell Biology

Background:

  • Singlet molecular oxygen (O2(a(1)Δg)) is involved in biological processes, including cell death.
  • Reactions between singlet oxygen and proteins can alter protein behavior.
  • The impact of protein structure on singlet oxygen behavior is understudied.

Purpose of the Study:

  • To investigate how protein structural changes affect the rate of singlet oxygen removal.
  • To explore the potential of using singlet oxygen kinetics to monitor protein dynamics.

Main Methods:

  • Studied the rate constant of singlet oxygen removal by various proteins.
  • Manipulated protein structure through denaturation, macromolecular crowding, ligand binding, and polymerization.

Main Results:

  • Protein denaturation, crowding, ligand binding, and polymerization significantly alter the rate constant for singlet oxygen removal.
  • Changes in protein structure that expose or hide amino acid residues measurably affect singlet oxygen quenching rates.

Conclusions:

  • Protein structural dynamics play a crucial role in modulating singlet oxygen reactivity.
  • Understanding these interactions is vital for comprehending singlet-oxygen-mediated cellular events and their impact on cell function.