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Related Concept Videos

Hydrolysis of ATP01:08

Hydrolysis of ATP

The bonds of adenosine triphosphate (ATP) can be broken through the addition of water, releasing one or two phosphate groups in an exergonic process called hydrolysis. This reaction liberates the energy in the bonds for use in the cell—for instance, to synthesize proteins from amino acids.
If one phosphate group is removed, a molecule of ADP—adenosine diphosphate—remains, along with inorganic phosphate. ADP can be further hydrolyzed to AMP—adenosine monophosphate—by the removal of a second...
Hydrolysis of ATP01:08

Hydrolysis of ATP

The bonds of adenosine triphosphate (ATP) can be broken through the addition of water, releasing one or two phosphate groups in an exergonic process called hydrolysis. This reaction liberates the energy in the bonds for use in the cell—for instance, to synthesize proteins from amino acids.
If one phosphate group is removed, a molecule of ADP—adenosine diphosphate—remains, along with inorganic phosphate. ADP can be further hydrolyzed to AMP—adenosine monophosphate—by the removal of a second...
ATP Energy Storage and Release01:31

ATP Energy Storage and Release

ATP is a highly unstable molecule. Unless quickly used to perform work, ATP spontaneously dissociates into ADP and inorganic phosphate (Pi), and the free energy released during this process is lost as heat. The energy released by ATP hydrolysis is used to perform work inside the cell and depends on a strategy called energy coupling. Cells couple the exergonic reaction of ATP hydrolysis with endergonic reactions, allowing them to proceed.
One example of energy coupling using ATP involves a...
ATP Energy Storage and Release01:31

ATP Energy Storage and Release

ATP is a highly unstable molecule. Unless quickly used to perform work, ATP spontaneously dissociates into ADP and inorganic phosphate (Pi), and the free energy released during this process is lost as heat. The energy released by ATP hydrolysis is used to perform work inside the cell and depends on a strategy called energy coupling. Cells couple the exergonic reaction of ATP hydrolysis with endergonic reactions, allowing them to proceed.
One example of energy coupling using ATP involves a...
Phosphodiester Linkages01:01

Phosphodiester Linkages

Overview
Phosphodiester bond forms when a phosphoric acid molecule (H3PO4) links with two hydroxyl groups (–OH) of two other molecules, forming two ester bonds. Two water molecules are released in this process. The phosphodiester bond is commonly found in nucleic acids (DNA and RNA) and plays a critical role in their structure and function.
Phosphodiester Bonds Link Nucleotides Together
DNA and RNA are polynucleotides or long chains of nucleotides that are linked together. A nucleotide is...
ATP Yield01:31

ATP Yield

Cellular respiration produces 30 - 32 ATP per glucose molecule. Although most of the ATP results from oxidative phosphorylation and the electron transport chain (ETC), 4 ATP are gained beforehand (2 from glycolysis and 2 from the citric acid cycle).
The ETC is embedded in the inner mitochondrial membrane and is comprised of four main protein complexes and an ATP synthase. NADH and FADH2 pass electrons to these complexes, which pump protons into the intermembrane space. This distribution of...

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Related Experiment Video

Updated: Jun 10, 2026

Chemical Triphosphorylation of Oligonucleotides
13:19

Chemical Triphosphorylation of Oligonucleotides

Published on: June 2, 2022

RIG-I "sees" the 5'-triphosphate.

Chao Zheng1, Hao Wu

  • 1Weill Medical College of Cornell University, New York, NY 10021, USA.

Structure (London, England : 1993)
|August 11, 2010
PubMed
Summary
This summary is machine-generated.

Retinoic acid-inducible gene I (RIG-I) detects viral RNA in cells. Its C-terminal domain recognizes the 5'-triphosphate group on double-stranded RNA, crucial for antiviral defense.

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Area of Science:

  • Immunology
  • Virology
  • Structural Biology

Background:

  • RIG-I is a key cytoplasmic sensor for viral RNA detection.
  • It initiates innate immune responses against RNA viruses.

Discussion:

  • The crystal structure reveals how RIG-I's C-terminal domain binds to 5 '-triphosphate dsRNA.
  • This binding mechanism highlights the recognition of the 5 '-triphosphate moiety as a viral RNA signature.

Key Insights:

  • Structural insights into RIG-I-dsRNA interaction.
  • Elucidation of the molecular basis for viral RNA recognition by RIG-I.

Outlook:

  • Understanding RIG-I function is vital for developing antiviral therapies.
  • Further structural studies can inform the design of novel immune-modulating drugs.