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Hydrogen bonds are weak attractions between atoms that have formed other chemical bonds. One of these atoms is electronegative, like oxygen, and has a partial negative charge. The other is a hydrogen atom that has bonded with another electronegative atom and has a partial positive charge.
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A hydrogen bond is formed when a weakly positive hydrogen atom already bonded to one electronegative atom (for example, the oxygen in the water molecule) is attracted to another electronegative atom from another polar molecule, such as water (H2O), hydrogen fluoride (HF), or ammonia (NH3). The huge electronegativity difference between the H atom (2.1) and the atom to which it is bonded (4.0 for an F atom, 3.5 for an O atom, or 3.0 for an N atom), combined with the very small size of an H atom...
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Sulfides are the sulfur analog of ethers, just as thiols are the sulfur analog of alcohol. Like ethers, sulfides also consist of two hydrocarbon groups bonded to the central sulfur atom. Depending upon the type of groups present, sulfides can be symmetrical or asymmetrical. Symmetrical sulfides can be prepared via an SN2 reaction between 2 equivalents of an alkyl halide and one equivalent of sodium sulfide.
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Information enters the brain through encoding, which is the input of information into the memory system. Once sensory information is received from the environment, the brain labels or codes it. The information is then organized with similar information and connected to existing concepts. Encoding occurs through automatic processing and effortful processing.
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Thiols and sulfides are sulfur analogs of alcohols and ethers, respectively, where the sulfur atom takes the place of the oxygen atom. Thus, thiols are generally represented as RSH, where R is an alkyl substituent and —SH is the functional group. On the other hand, in sulfides, the central sulfur atom is bonded to two hydrocarbon groups on either side. Depending upon the type of group, sulfides can be either symmetrical or asymmetrical. Both thiols and sulfides display a bent geometry,...
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Among all the organelles in an animal cell, only mitochondria have their own independent genomes. Animal mitochondrial DNA is a double-stranded, closed-circular molecule with around 20,000 base pairs. Mitochondrial DNA is unique in that one of its two strands, the heavy, or H, -strand is guanine rich, whereas the complementary strand is cytosine rich and called the light, or L, -strand. Compared to nuclear DNA, mitochondrial DNA has a very low percentage of non-coding regions and is marked by...
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A Genetically Encoded, Ratiometric Fluorescent Biosensor for Hydrogen Sulfide.

Suzan Youssef1, Shen Zhang2, Hui-Wang Ai1,2

  • 1Department of Chemistry , University of California , 501 Big Springs Road , Riverside , California 92521 , United States.

ACS Sensors
|May 16, 2019
PubMed
Summary

Researchers developed hsFRET, the first ratiometric biosensor for hydrogen sulfide (H2S). This genetically encoded tool uses fluorescence resonance energy transfer (FRET) for precise H2S detection in cells and in vitro.

Keywords:
Förster resonance energy transferfluorescent protein-based biosensorgenetic code expansionhydrogen sulfideratiometric measurementunnatural amino acid

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Signaling

Background:

  • Hydrogen sulfide (H2S) is a vital gasotransmitter involved in cellular signaling pathways.
  • Genetically encoded fluorescent biosensors, utilizing p-azidophenylalanine (pAzF) incorporation, have enabled intensity-based detection of H2S.
  • Ratiometric measurements offer enhanced accuracy by minimizing detection variability through self-calibration.

Purpose of the Study:

  • To develop the first ratiometric, genetically encoded fluorescent biosensor for hydrogen sulfide (H2S).
  • To enable more precise and reliable monitoring of H2S levels in biological systems.

Main Methods:

  • Genetic code expansion was used to incorporate p-azidophenylalanine (pAzF) into a circularly permutated superfolder green fluorescent protein (cpsGFP).
  • The modified protein (cpsGFP-pAzF) was engineered to act as a Förster resonance energy transfer (FRET) acceptor for enhanced blue fluorescent protein (EBFP2).
  • The resulting construct, hsFRET, was tested for its ability to detect H2S in vitro and in mammalian cells.

Main Results:

  • The hsFRET biosensor demonstrated a ratiometric response to H2S.
  • H2S was shown to reduce the azido group of hsFRET to an amine, altering FRET efficiency.
  • An increase in FRET from EBFP2 to cpsGFP was observed upon H2S exposure, indicating successful detection.

Conclusions:

  • hsFRET represents the first ratiometric, genetically encoded fluorescent biosensor for H2S.
  • This novel biosensor allows for selective and ratiometric monitoring of H2S.
  • The hsFRET system provides a valuable tool for studying H2S in biological contexts.