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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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Phosphate Buffer01:22

Phosphate Buffer

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The phosphate buffer system is a critical biological mechanism for maintaining pH stability in the body. This system operates primarily through two components: sodium dihydrogen phosphate (NaH2PO4), which acts as a weak acid, and sodium hydrogen phosphate (Na2HPO4), which serves as a weak base.
Sodium dihydrogen phosphate does not fully dissociate in neutral or acidic solutions. When a strong base, such as sodium hydroxide (NaOH), is introduced into the solution, sodium dihydrogen phosphate...
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Other Nuclides: 31P, 19F, 15N NMR01:16

Other Nuclides: 31P, 19F, 15N NMR

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Many organic, inorganic, and biological molecules contain spin-half nuclei such as nitrogen-15, fluorine-19, and phosphorus-31. As a result, NMR studies of these nuclei have found extensive applications in chemical and biological research.
While fluorine-19 and phosphorous-31 have high natural abundances (100%) and positive gyromagnetic ratios, nitrogen-15 has a low natural abundance and a negative gyromagnetic ratio. However, nitrogen-15 is still preferred over nitrogen-14 (which has a...
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Phosphorylation01:02

Phosphorylation

54.7K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
54.7K
Polyprotic Acids03:38

Polyprotic Acids

32.3K
Acids are classified by the number of protons per molecule that they can give up in a reaction. Acids such as HCl, HNO3, and HCN that contain one ionizable hydrogen atom in each molecule are called monoprotic acids. Their reactions with water are:
32.3K
ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

10.0K
ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and...
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Related Experiment Video

Updated: Feb 24, 2026

Investigating Cardiac Metabolism in the Isolated Perfused Mouse Heart with Hyperpolarized [1-13C]Pyruvate and 13C/31P NMR Spectroscopy
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Investigating Cardiac Metabolism in the Isolated Perfused Mouse Heart with Hyperpolarized [1-13C]Pyruvate and 13C/31P NMR Spectroscopy

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Biochemical phosphates observed using hyperpolarized 31P in physiological aqueous solutions.

Atara Nardi-Schreiber1, Ayelet Gamliel1, Talia Harris1

  • 1Department of Radiology, Hadassah-Hebrew University Medical Center, Jerusalem, Israel.

Nature Communications
|August 26, 2017
PubMed
Summary

Hyperpolarized 31P nuclear magnetic resonance (NMR) can now detect biological phosphates like inorganic phosphate and phosphocreatine. This breakthrough enables real-time monitoring of phosphate metabolism and pH sensing in vivo without ionizing radiation.

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Phosphorus-31 Magnetic Resonance Spectroscopy: A Tool for Measuring In Vivo Mitochondrial Oxidative Phosphorylation Capacity in Human Skeletal Muscle
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Optimized Procedure for Determining the Adsorption of Phosphonates onto Granular Ferric Hydroxide using a Miniaturized Phosphorus Determination Method
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Optimized Procedure for Determining the Adsorption of Phosphonates onto Granular Ferric Hydroxide using a Miniaturized Phosphorus Determination Method

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Related Experiment Videos

Last Updated: Feb 24, 2026

Investigating Cardiac Metabolism in the Isolated Perfused Mouse Heart with Hyperpolarized [1-13C]Pyruvate and 13C/31P NMR Spectroscopy
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Investigating Cardiac Metabolism in the Isolated Perfused Mouse Heart with Hyperpolarized [1-13C]Pyruvate and 13C/31P NMR Spectroscopy

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Phosphorus-31 Magnetic Resonance Spectroscopy: A Tool for Measuring In Vivo Mitochondrial Oxidative Phosphorylation Capacity in Human Skeletal Muscle
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Optimized Procedure for Determining the Adsorption of Phosphonates onto Granular Ferric Hydroxide using a Miniaturized Phosphorus Determination Method
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Optimized Procedure for Determining the Adsorption of Phosphonates onto Granular Ferric Hydroxide using a Miniaturized Phosphorus Determination Method

Published on: May 18, 2018

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Area of Science:

  • Nuclear Magnetic Resonance Spectroscopy
  • Biophysical Chemistry
  • Medical Imaging

Background:

  • Dissolution-dynamic nuclear polarization (DNP) enhances NMR sensitivity for various nuclei.
  • Real-time in vivo monitoring of phosphate metabolism and pH is crucial for understanding biological processes.

Purpose of the Study:

  • To demonstrate hyperpolarization of 31P nuclei in biological phosphates (inorganic phosphate, phosphocreatine) using DNP.
  • To explore the potential of hyperpolarized 31P NMR for real-time biological monitoring.

Main Methods:

  • Utilized dissolution-dynamic nuclear polarization technology to achieve hyperpolarization of 31P nuclei.
  • Investigated hyperpolarized inorganic phosphate and phosphocreatine in aqueous solutions.
  • Analyzed the effects of deuteration, solution composition, and pH on the hyperpolarized state's lifetime.

Main Results:

  • Achieved significant signal enhancement (>11,000) for hyperpolarized inorganic phosphate.
  • Demonstrated the influence of environmental factors (deuteration, pH) on the T1 relaxation time.
  • Successfully detected immediate pH changes in a cell-free system using the chemical shift of hyperpolarized inorganic phosphate.

Conclusions:

  • Hyperpolarized 31P NMR of biological phosphates is feasible and offers high sensitivity.
  • This technique facilitates non-ionizing, real-time monitoring of phosphate metabolism, distribution, and pH sensing.
  • The 100% natural abundance of 31P eliminates the need for isotopic labeling, reducing costs for future studies.