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Related Concept Videos

Phosphorylation01:02

Phosphorylation

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...
Phosphorylation01:02

Phosphorylation

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...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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...
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...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

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Related Experiment Video

Updated: May 19, 2026

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins
10:54

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

Published on: May 30, 2025

Why nature chose phosphate to modify proteins.

Tony Hunter1

  • 1Salk Institute for Biological Studies, La Jolla, CA 92037, USA. hunter@salk.edu

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
|August 15, 2012
PubMed
Summary

Phosphorylation, a key post-translational modification, diversifies protein surfaces and enables signal transduction. This reversible process creates unique phosphoamino acids, crucial for cellular communication and response to stimuli.

Related Experiment Videos

Last Updated: May 19, 2026

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins
10:54

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

Published on: May 30, 2025

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • The phosphate ester linkage is fundamental in nucleic acids (RNA and DNA).
  • Protein phosphorylation evolved as a prominent post-translational modification.
  • Phosphorylation modifies hydroxyamino acids: serine, threonine, and tyrosine.

Purpose of the Study:

  • To explore the evolutionary significance and biochemical roles of protein phosphorylation.
  • To understand how phosphorylation diversifies protein function and facilitates signal transduction.

Main Methods:

  • The study is primarily a review and synthesis of existing knowledge on phosphorylation.
  • Analysis of the chemical properties and evolutionary origins of phosphate ester linkages.

Main Results:

  • Phosphorylation generates novel phosphoamino acids, altering protein surface chemistry.
  • Phosphate groups form specific interactions (hydrogen bonds, salt bridges) with amino acids like arginine.
  • Phosphorylation enables inducible protein-protein interactions via phosphospecific-binding domains.

Conclusions:

  • Protein phosphorylation is a versatile and reversible modification essential for signal transduction.
  • It acts as a molecular switch, allowing cells to respond to external signals.
  • The unique chemical properties of phosphate drive its diverse biological roles.