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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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Role of Proteins in the Human Body01:28

Role of Proteins in the Human Body

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Proteins are the building block of life. They are also  the most abundant macromolecules with as many diverse roles in the body. They are part of many structural components that provide unique shapes and structures to animal cells, tissues, and organs. In addition, they also act as biological catalysts and carry out several anabolic and catabolic reactions. Notably, some proteins are chemical messengers and regulate many critical processes, such as metabolism, growth, and development. They...
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What are Proteins?01:28

What are Proteins?

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Proteins are polymers of amino acids linked together by peptide bonds. Proteins and polypeptides are interchangeably used to refer to long chains of amino acids. However, polypeptides have a molecular weight of fewer than 10,000 daltons, while proteins have greater molecular weight.  Polypeptides with less than 20 amino acids are called oligopeptides or simply peptides. Interactions among the constituent amino acid side chains of proteins help them fold into a stable 3-dimensional...
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Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

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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.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
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Protein Digestion01:02

Protein Digestion

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Protein digestion begins in the stomach, where the highly acidic environment can easily disrupt protein structure by exposing the peptide bonds of polypeptide chains. After polypeptide chains are broken into individual amino acids by a series of digestive enzymes, the amino acids are transported to the liver via the bloodstream to produce energy.
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Protein Organization01:24

Protein Organization

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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.
The primary structure of a protein is its amino acid sequence....
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A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
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A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

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Peptides - Molecular Allrounders.

Helma Wennemers1

  • 1Laboratorium für Organische Chemie, ETH Zürich, D-CHAB, Vladimir-Prelog-Weg 3, CH-8093 Zurich;,

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|July 8, 2021
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Summary
This summary is machine-generated.

Researchers developed novel peptide catalysts and materials for diverse applications. This work explores bioinspired catalysis, synthetic collagen, porous assemblies, and cell-penetrating peptides, showcasing peptide chemistry

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Area of Science:

  • Peptide Chemistry
  • Asymmetric Catalysis
  • Supramolecular Chemistry
  • Chemical Biology

Background:

  • Peptides offer vast structural and functional diversity.
  • Amino acid combinations create unique molecular properties.
  • Current research explores advanced peptide applications.

Purpose of the Study:

  • To highlight recent laboratory research in peptide science.
  • To showcase advancements in bioinspired catalysis and supramolecular chemistry.
  • To present novel synthetic peptides for various applications.

Main Methods:

  • Development of bioinspired peptide catalysts.
  • Synthesis of collagen-mimetic peptides.
  • Construction of supramolecular porous assemblies.
  • Design of cell-penetrating peptides.

Main Results:

  • Successful creation of novel peptide-based catalysts.
  • Generation of synthetic collagen peptides with tailored properties.
  • Fabrication of functional supramolecular porous materials.
  • Engineering of peptides for enhanced cellular uptake.

Conclusions:

  • Peptide chemistry provides a versatile platform for innovation.
  • The developed peptides show promise in catalysis, materials science, and cell biology.
  • Future research can leverage these findings for new therapeutic and material applications.