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Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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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...
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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. 
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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
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Related Experiment Video

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Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
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Progress and challenges in simulating and understanding electron transfer in proteins.

Aurélien de la Lande1, Natacha Gillet1, Shufeng Chen1

  • 1Laboratoire de Chimie Physique, UMR 8000, CNRS, Université Paris Sud. 15, av. Jean Perrin, 91405 Orsay, France.

Archives of Biochemistry and Biophysics
|June 28, 2015
PubMed
Summary

This review explores numerical simulations for electron transfer (ET) in proteins. It covers direct simulation algorithms, Marcus theory applications, and quantum chemistry methods for tunneling, highlighting current capabilities and challenges in protein biophysics.

Keywords:
Electron transfersMarcus theoryNumerical simulationsProteinsTunelling

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Area of Science:

  • Biophysics
  • Computational Chemistry
  • Biochemistry

Background:

  • Electron transfer (ET) is crucial in biological processes.
  • Understanding ET mechanisms in proteins requires advanced computational methods.
  • Current simulation techniques face limitations in accuracy and scope.

Purpose of the Study:

  • To provide a comprehensive overview of numerical simulation approaches for ET in proteins.
  • To discuss the strengths, limitations, and challenges of various simulation methods.
  • To illustrate the application of these methods with literature examples.

Main Methods:

  • Direct simulation algorithms for charge migration.
  • Methods for testing Marcus theory and evaluating thermodynamic quantities (reorganization energies, driving force).
  • Quantum chemistry approaches for electronic coupling and tunneling phenomena.

Main Results:

  • Overview of simulation techniques for protein ET.
  • Discussion of Marcus theory applicability and limitations (non-ergodic effects, non-linear responses).
  • Insights into electronic coupling and protein dynamics impact on tunneling.

Conclusions:

  • Atomistic simulations have advanced the understanding of protein ET biophysics.
  • Current methodologies allow for the investigation of various protein systems.
  • Further development is needed to address existing challenges in ET simulations.