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Related Concept Videos

Amino acids03:42

Amino acids

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Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible for...
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Amino Acid Catabolism01:18

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Microorganisms rely on proteins as an essential carbon and energy source, particularly in environments with limited polysaccharides or lipids. However, proteins are too large to cross the plasma membrane unaided, necessitating enzymatic degradation. Microbes secrete extracellular proteases and peptidases that hydrolyze proteins into peptides, which can then be transported across the membrane. Once inside the cell, intracellular proteases degrade these peptides into free amino acids, which...
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Amino Acid Biosynthetic Pathways01:29

Amino Acid Biosynthetic Pathways

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Amino acid biosynthesis is essential for cell growth, protein synthesis, and metabolic regulation. Cells generate essential and non-essential amino acids from metabolic intermediates to sustain vital biological functions. These intermediates originate from key metabolic pathways: glycolysis, the tricarboxylic acid (TCA) cycle, and the pentose phosphate pathway. Important precursors include α-ketoglutarate, pyruvate, oxaloacetate, phosphoenolpyruvate, and erythrose-4-phosphate, which...
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Solution Equilibrium and Saturation01:59

Solution Equilibrium and Saturation

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Imagine adding a small amount of sugar to a glass of water, stirring until all the sugar has dissolved, and then adding a bit more. You can repeat this process until the sugar concentration of the solution reaches its natural limit, a limit determined primarily by the relative strengths of the solute-solute, solute-solvent, and solvent-solvent attractive forces. You can be certain that you have reached this limit because, no matter how long you stir the solution, undissolved sugar remains. The...
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¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

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When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...
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NMR and Mass Spectroscopy of Carboxylic Acids01:30

NMR and Mass Spectroscopy of Carboxylic Acids

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In ¹H NMR spectroscopy, acidic protons (–COOH) of carboxylic acids are highly deshielded and absorb far downfield, at around 9–12 ppm. The chemical shift value depends on the concentration and solvent used.
While α protons of carboxylic acids absorb at 2–2.5 ppm, β protons absorb further upfield.
Carboxylic acids are easily identified by dissolving them in deuterium oxide, which results in a rapid exchange of the acidic protons with deuterium. This leads to the...
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Spin Saturation Transfer Difference NMR SSTD NMR: A New Tool to Obtain Kinetic Parameters of Chemical Exchange Processes
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Probing Amino Acid Interaction with a Polystyrene Nanoparticle Surface Using Saturation-Transfer Difference

Yunzhi Zhang1, Leah B Casabianca1

  • 1Department of Chemistry , Clemson University , Clemson , South Carolina 29634 , United States.

The Journal of Physical Chemistry Letters
|November 28, 2018
PubMed
Summary

This study used Saturation-Transfer Difference Nuclear Magnetic Resonance (STD-NMR) to investigate amino acid interactions with carboxylate-modified polystyrene nanoparticles, revealing binding modes like electrostatic, hydrophobic, and pi-pi interactions.

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Area of Science:

  • Biophysical Chemistry
  • Materials Science
  • Nanotechnology

Background:

  • Understanding nanoparticle-biomolecule interactions is crucial for applications in drug delivery and diagnostics.
  • Polystyrene nanoparticles are widely used, but their surface interactions with amino acids require detailed characterization.

Purpose of the Study:

  • To elucidate the binding mechanisms of individual amino acids to carboxylate-modified polystyrene nanoparticles.
  • To identify the dominant interaction modes based on amino acid side chain properties.

Main Methods:

  • Utilized Saturation-Transfer Difference Nuclear Magnetic Resonance (STD-NMR) spectroscopy.
  • Screened individual amino acids for nanoparticle binding and measured STD buildup curves.
  • Analyzed STD effects based on proton environments within amino acid side chains.

Main Results:

  • Strongest STD effects observed for protons of aromatic side chains, indicating significant binding.
  • Weaker STD effects detected for long-chain aliphatic and positively charged side chains.
  • Identified electrostatic attraction, hydrophobic effects, and π-π interactions as key binding modes.

Conclusions:

  • The binding of amino acids to carboxylate-modified polystyrene nanoparticles is multifaceted, involving electrostatic, hydrophobic, and π-π interactions.
  • Side chain chemistry dictates the dominant binding mode.
  • Findings provide a foundation for predicting interactions between nanoparticles and peptides/proteins.