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Related Concept Videos

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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Protein Organization01:24

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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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Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
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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.
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Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library
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A Structuring Repeat for Peptide Design: Long Beta Ribbons.

Brandon L Kier1, Gregory M Newbloom2, Lilo D Pozzo2

  • 1Department of Chemistry, University of Washington, Box 351700, Bagley Hall, Seattle, WA, 98195-1700, USA. sciguy@u.washington.edu.

Chembiochem : a European Journal of Chemical Biology
|November 26, 2015
PubMed
Summary
This summary is machine-generated.

Researchers developed a new method to extend beta sheets to any length using a stabilizing repeat unit. This breakthrough allows for the creation of significantly longer beta ribbons, overcoming inherent length limitations.

Keywords:
beta-capsbeta-sheetsbioengineeringdisulfidepeptide

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Engineering

Background:

  • Beta sheets have inherent length limitations, making it difficult to extend them beyond a certain size.
  • Traditional methods of adding residues to beta sheet ends do not effectively increase their length.

Purpose of the Study:

  • To present a novel method for extending beta sheets to arbitrary lengths.
  • To overcome the inherent length limitations of beta sheets.

Main Methods:

  • Introduction of a stabilizing repeat unit containing cross-strand Tryptophan (Trp) residues.
  • Engineering of beta ribbons using this repeat unit.

Main Results:

  • Successfully extended beta sheets to lengths of up to 35 residues.
  • Characterization of beta ribbons approaching 100 Å in length.
  • Demonstration of a method for creating long beta sheets.

Conclusions:

  • The developed method effectively extends beta sheets beyond inherent length limitations.
  • The stabilizing repeat unit is key to creating long and stable beta ribbons.
  • This technique opens possibilities for designing novel protein structures.