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Related Concept Videos

Protein Folding01:25

Protein Folding

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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
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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.
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Protein Modifications in the RER01:26

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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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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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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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Peptide Bonds02:43

Peptide Bonds

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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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Related Experiment Video

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Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
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Folding-Assisted Peptide Disulfide Formation and Dimerization.

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  • 1Department of Chemistry, Fordham University, 441 E. Fordham Rd., Bronx, New York 10458, United States.

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Controlling thiol oxidation conditions allows selective formation of disulfide bonds in peptides. This method can yield either monomeric or dimeric species, influencing peptide folding and stability for various applications.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Chemical Synthesis and Peptide Chemistry

Background:

  • Disulfide bonds are crucial covalent linkages in peptides and proteins, significantly affecting their structure, stability, and oligomerization.
  • Controlling disulfide bond formation is vital for understanding and engineering peptide and protein folding, particularly in chemically synthesized molecules.

Purpose of the Study:

  • To investigate how varying thiol oxidation conditions influence the folding and oligomerization of linear bisthiol peptides.
  • To demonstrate a method for controlling the formation of specific disulfide bond architectures (monomeric vs. dimeric) in peptides.

Main Methods:

  • Site-selective disulfide bond formation via controlled thiol oxidation of fully deprotected linear bisthiol peptides.
  • Comparative analysis of peptide species formed under aqueous (nondenaturing) versus denaturing oxidation conditions.
  • Assessment of peptide variants to determine factors influencing intramolecular disulfide formation and dimerization.

Main Results:

  • Nondenaturing aqueous oxidation of a p53-derived peptide yielded antiparallel dimers with increased alpha-helical content.
  • Denaturing oxidation conditions favored the formation of nonhelical intramolecular disulfide species.
  • Intramolecular disulfide formation proved robust across different peptide sequences, while dimerization depended on peptide helical folding and aromatic residues.

Conclusions:

  • Thiol oxidation conditions can be strategically employed to control peptide oligomerization and folding through disulfide bond formation.
  • The resulting disulfide-bonded peptides exhibit enhanced protease resistance compared to their linear counterparts.
  • This approach offers a versatile tool for studying peptide folding, oligomerization, and interactions with molecular targets.