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Peptide Bonds02:43

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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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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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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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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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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
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Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
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Electron transfer in peptides.

Afzal Shah1, Bimalendu Adhikari, Sanela Martic

  • 1Department of Physical and Environmental Sciences, University of Toronto Scarborough, 1265 Military Trail, Toronto, M1C 1A4, Canada. bernie.kraatz@utoronto.ca afzals_qau@yahoo.com.

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Electron transfer in peptides is influenced by various factors beyond chain length. Understanding these mechanisms is crucial for applications in bioelectrochemical systems and molecular electronics.

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Area of Science:

  • Biophysics
  • Chemical Physics
  • Molecular Biology

Background:

  • Electron transfer is fundamental to many physical, chemical, and biological processes.
  • Peptides play a significant role in mediating electron transfer reactions.
  • The precise mechanisms governing electron transfer in peptides are still debated.

Purpose of the Study:

  • To review factors influencing electron transfer in peptides.
  • To summarize experimental findings from solution and surface studies.
  • To present a balanced view of the mechanistic aspects of peptide electron transfer.

Main Methods:

  • Literature review of experimental results.
  • Analysis of solution and surface studies.
  • Contrasting different proposed electron transfer mechanisms.

Main Results:

  • Electron transfer mechanisms in peptides include hopping, tunneling, ballistic, and pathway transfer.
  • Mechanism can change with donor-acceptor separation and is not solely dependent on chain length.
  • Secondary structure, conformation, amino acid composition, and dynamics significantly affect electron transfer.

Conclusions:

  • Factors beyond simple chain length, such as peptide structure and dynamics, are critical for electron transfer.
  • A comprehensive understanding of these factors is essential for controlling electron transfer in peptides.
  • This knowledge is vital for developing peptide-based sensors and molecular junctions.