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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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Peptide Identification Using Tandem Mass Spectrometry01:33

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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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Co-activators and Co-repressors02:04

Co-activators and Co-repressors

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Gene transcription is regulated by the synergistic action of several proteins that form a complex at a gene regulatory site. This is observed in eukaryotes, where the regulation of gene expression is a complex process. Regulatory proteins in eukaryotes can broadly be classified into two types – regulators that bind directly to specific DNA sequences and co-regulators that associate with regulatory proteins but cannot directly bind to the DNA. These co-regulators are further divided into...
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tRNA Activation02:26

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Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
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Activation Energy01:26

Activation Energy

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Activation energy is the minimum amount of energy necessary for a chemical reaction to move forward. The higher the activation energy, the slower the rate of the reaction. However, adding heat to the reaction will increase the rate, since it causes molecules to move faster and increase the likelihood that molecules will collide. The collision and breaking of bonds represents the uphill phase of a reaction and generates the transition state. The transition state is an unstable high-energy state...
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Eukaryotic Transcription Activators02:42

Eukaryotic Transcription Activators

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Transcription activators are proteins that promote the transcription of genes from DNA to RNA. In most cases, these proteins contain two separate domains ‒ a domain that binds to DNA and a domain for activating transcription; however, in some cases, a single domain is responsible for both binding and activation of transcription, as seen in the glucocorticoid receptor and MyoD.
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Protein Kinase C-delta Inhibitor Peptide Formulation using Gold Nanoparticles
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Peptide-Programmable Nanoparticle Superstructures with Tailored Electrocatalytic Activity.

Eun Sung Kang1, Yong-Tae Kim1, Young-Seon Ko1

  • 1SKKU Advanced Institute of Nanotechnology (SAINT) , Sungkyunkwan University , Suwon 16419 , Republic of Korea.

ACS Nano
|May 30, 2018
PubMed
Summary
This summary is machine-generated.

Researchers created precise nanoparticle superstructures on carbon nanotubes using peptide assembly. This biomaterial design enables distinct electrocatalytic activities based on nanoparticle arrangement, paving the way for advanced functional materials.

Keywords:
artificialy designed peptideelectrocatalytic oxygen reductionelectron tomographynanoparticle superstructurepeptide-based catalystpeptide-based superstructure 3-D reconstructionsupramolecular protein self-assembly

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Area of Science:

  • Biomaterials science
  • Nanotechnology
  • Supramolecular chemistry

Background:

  • Programmable supramolecular protein assembly offers precise control over biomaterial structure.
  • Developing methods for constructing complex nanomaterials with tailored properties is crucial.

Purpose of the Study:

  • To present programmed superstructures of gold-platinum nanoparticles (AuPt NPs) on carbon nanotubes (CNTs) using peptide-mediated assembly.
  • To demonstrate distinct electrocatalytic activities based on controlled nanoparticle positioning.

Main Methods:

  • De novo designed peptides were used to form six-helix bundles along CNTs, creating a suprahelical structure.
  • Surface cysteine residues on peptides acted as nucleation sites for precise AuPt NP positioning.
  • Three-dimensional reconstruction via electron tomography confirmed NP arrangement.

Main Results:

  • Precisely positioned AuPt NPs were successfully assembled onto helical peptide structures on CNTs.
  • The resulting superstructures exhibited distinct electrocatalytic activities for oxygen reduction, correlating with NP arrangement.
  • Electrochemical response signals validated the controlled assembly of NPs.

Conclusions:

  • Peptide-mediated assembly provides a versatile platform for creating sophisticated, precisely defined nanomaterial superstructures.
  • This approach allows for rational modulation of functional properties, such as electrocatalysis, based on structural design.
  • The methodology is adaptable for diverse applications requiring complex functional assemblies.