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Related Concept Videos

Mechanical Protein Functions01:58

Mechanical Protein Functions

Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
Electron Transport Chain Components01:29

Electron Transport Chain Components

The electron transport chain (ETC) is a crucial metabolic pathway that facilitates energy conversion in prokaryotic and eukaryotic cells. In eukaryotes, the ETC comprises four membrane-associated protein complexes in the inner mitochondrial membrane. In prokaryotes, the ETC in the plasma membrane can vary in composition, with fewer or different complexes depending on the organism and environmental conditions. These complexes transfer electrons from electron donors, such as NADH and FADH2, to...
Energy to Drive Translocation01:37

Energy to Drive Translocation

Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
Chemiosmosis and ATP Synthesis01:22

Chemiosmosis and ATP Synthesis

The electron transport chain is a critical component of cellular respiration, occurring in the inner mitochondrial membrane. It facilitates the transfer of high-energy electrons from reduced cofactors NADH and FADH₂ to molecular oxygen, the final electron acceptor. This transfer of electrons through a series of protein complexes is tightly coupled to the translocation of protons across the membrane, generating a proton gradient essential for ATP synthesis.Electron Flow and Proton...
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
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...

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Related Experiment Video

Updated: Jul 6, 2026

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
10:50

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Published on: March 14, 2019

Energy flow in proteins.

David M Leitner1

  • 1Department of Chemistry and Chemical Physics Program, University of Nevada, Reno, Nevada 89557, USA. dml@chem.unr.edu

Annual Review of Physical Chemistry
|April 9, 2008
PubMed
Summary
This summary is machine-generated.

Energy moves directionally through protein structures, forming channels that can link functional sites. This anisotropic energy flow in globular proteins is similar to transport in disordered systems like percolation clusters.

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Last Updated: Jul 6, 2026

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
10:50

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Published on: March 14, 2019

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Area of Science:

  • Biophysics
  • Protein dynamics
  • Disordered systems

Background:

  • Energy transport in globular proteins is anisotropic.
  • Energy transport channels exist within proteins, sometimes connecting functional regions.
  • This transport can be modeled using percolation clusters.

Purpose of the Study:

  • To review connections between globular proteins and percolation clusters.
  • To examine the similarity of energy and thermal transport in these systems.
  • To review studies on anisotropic energy flow in protein vibrational states.

Main Methods:

  • Review of experimental studies on protein energy transport.
  • Review of computational studies on protein energy transport.
  • Comparison with transport on percolation clusters and disordered systems.

Main Results:

  • Energy flow in proteins is anisotropic, occurring through specific residues and vibrational states.
  • Protein energy transport shares similarities with transport on percolation clusters.
  • Anisotropic energy flow can be understood by comparing proteins to simple disordered systems.

Conclusions:

  • Anisotropic energy flow is a key property of globular proteins.
  • Percolation theory provides a useful model for understanding energy transport in proteins.
  • Further research into protein dynamics and energy transport is warranted.