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Related Concept Videos

ATP and Macromolecule Synthesis01:28

ATP and Macromolecule Synthesis

6.8K
Biological macromolecules are organic compounds, predominantly composed of carbon atoms. The carbon atoms are covalently bonded with hydrogen, oxygen, nitrogen, and other minor elements. There are four major biological macromolecule classes: carbohydrates, lipids, proteins, and nucleic acids.
Most macromolecules are composed of single subunits, or building blocks, called monomers. The monomers combine with each other using covalent bonds to form larger molecules known as polymers.
Conversion of...
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ATP Energy Storage and Release01:31

ATP Energy Storage and Release

13.9K
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...
13.9K
ATP Synthase: Structure01:18

ATP Synthase: Structure

15.1K
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
15.1K
Hydrolysis of ATP01:08

Hydrolysis of ATP

81.0K
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...
81.0K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

16.7K
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
16.7K
ATP and Energy Production01:23

ATP and Energy Production

1.6K
Adenosine triphosphate (ATP) is a critical molecule that functions as the main energy carrier in cells. Structurally, ATP consists of an adenosine molecule—comprising adenine and ribose—bonded to three phosphate groups. The high-energy bonds between these phosphate groups store significant amounts of potential energy. This energy is released during hydrolysis, wherein ATP is converted to adenosine diphosphate (ADP) or adenosine monophosphate (AMP), driving a variety of essential...
1.6K

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Related Experiment Video

Updated: Jan 15, 2026

Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins
07:25

Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins

Published on: October 17, 2014

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ATP Can Act as a Stabilizer on Neutral Macromolecules.

Cansin Ayvaz1, Yaren S Ozdogan1, Dilsad S Peker1

  • 1Department of Chemistry, Faculty of Science, Bilkent University, 06800 Ankara, Turkey.

The Journal of Physical Chemistry Letters
|October 7, 2025
PubMed
Summary

Adenosine triphosphate (ATP) acts as a hydrotrope, influencing macromolecule phase transitions. At physiological concentrations, ATP stabilizes macromolecules via an excluded volume effect, contrary to its destabilizing action on protein coacervates.

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Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
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Last Updated: Jan 15, 2026

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Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
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Area of Science:

  • Biochemistry
  • Physical Chemistry
  • Polymer Science

Background:

  • Adenosine triphosphate (ATP) is crucial for cellular energy and has recently been identified as a hydrotrope.
  • ATP's hydrotropic role, particularly in destabilizing protein coacervates, requires further mechanistic investigation.
  • Understanding ATP's interaction with macromolecules is key to elucidating its diverse biological functions.

Purpose of the Study:

  • To investigate the influence of ATP and related molecules on macromolecular phase transitions.
  • To explore the mechanism behind ATP's hydrotropic action on poly(N-isopropylacrylamide) (PNIPAM).
  • To determine the concentration-dependent effects of ATP on macromolecule solubility and aggregation.

Main Methods:

  • Utilized Lower Critical Solution Temperature (LCST) and spectroscopic techniques (1H NMR, ATR-FTIR).
  • Employed solvation shell spectroscopy and all-atom molecular dynamics (MD) simulations.
  • Analyzed the effects of adenine, adenosine, AMP, triphosphate (TP), and ATP on PNIPAM.

Main Results:

  • ATP, AMP, and triphosphate promoted macromolecule aggregation (salting-out effect), while adenine and adenosine had minimal impact.
  • ATR-FTIR confirmed salting-out behavior at physiological ATP concentrations (<0.1 M).
  • No specific binding interactions were detected between PNIPAM and ATP via spectroscopy or MD simulations; ATP self-associates at higher concentrations.

Conclusions:

  • ATP's hydrotropic action is dependent on macromolecule structure and concentration.
  • At physiological concentrations, ATP stabilizes neutral macromolecules through an excluded volume effect, not by direct binding.
  • The findings clarify ATP's role in macromolecular behavior, distinct from its effect on protein coacervates.