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Related Concept Videos

Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

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...
Peptide Bonds02:43

Peptide Bonds

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...
Protein Folding01:25

Protein Folding

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
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...
Protein Digestion01:02

Protein Digestion

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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Related Experiment Video

Updated: May 20, 2026

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
10:42

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

New materials from proteins and peptides.

Tijana Z Grove1, Lynne Regan

  • 1Department of Chemistry, Virginia Tech, Blacksburg, VA 24060, USA.

Current Opinion in Structural Biology
|July 27, 2012
PubMed
Summary

Researchers are designing advanced protein and peptide materials, including responsive hydrogels and composite protein materials. These novel biomaterials show promise for various practical applications due to their unique tunable properties.

Area of Science:

  • Biomaterials Science
  • Protein Engineering
  • Polymer Chemistry

Background:

  • Proteins and peptides offer unique building blocks for advanced materials.
  • Designing protein-based materials allows for precise control over structure and function.
  • Natural protein segments can be combined to create materials with emergent properties.

Purpose of the Study:

  • To review recent advancements in designing materials from proteins and peptides.
  • To highlight examples of innovative protein-based material designs.
  • To consider the practical applications of these novel biomaterials.

Main Methods:

  • Design and synthesis of aggregating beta-hairpin peptides for hydrogels.
  • Combinatorial assembly of natural elastomeric protein segments (elastin, resilin, silk fibroin).

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Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy
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Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy

Published on: March 6, 2017

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Related Experiment Videos

Last Updated: May 20, 2026

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
10:42

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy
05:44

Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy

Published on: March 6, 2017

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

  • Creation of protein module hydrogels cross-linked by peptide ligands.
  • Main Results:

    • Designed beta-hairpin peptide hydrogels exhibit tunable physical properties based on amino acid changes.
    • Composite protein materials show bulk properties influenced unexpectedly by their composition.
    • Protein module hydrogels demonstrate exquisite stimuli-responsive behavior.

    Conclusions:

    • Protein and peptide-based materials offer versatile platforms for advanced applications.
    • Precise design of protein materials enables tailored functionalities.
    • Further exploration of these biomaterials is warranted for practical implementation.