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Related Concept Videos

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.
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.
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...
What are Proteins?01:28

What are Proteins?

Proteins are polymers of amino acids linked together by peptide bonds. Proteins and polypeptides are interchangeably used to refer to long chains of amino acids. However, polypeptides have a molecular weight of fewer than 10,000 daltons, while proteins have greater molecular weight.  Polypeptides with less than 20 amino acids are called oligopeptides or simply peptides. Interactions among the constituent amino acid side chains of proteins help them fold into a stable 3-dimensional structure...
What are Proteins?01:55

What are Proteins?

Overview

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Related Experiment Video

Updated: May 13, 2026

Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations
05:57

Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations

Published on: April 26, 2024

Considering protonation as a posttranslational modification regulating protein structure and function.

André Schönichen1, Bradley A Webb, Matthew P Jacobson

  • 1Department of Cell and Tissue Biology, University of California, San Francisco, USA.

Annual Review of Biophysics
|March 5, 2013
PubMed
Summary
This summary is machine-generated.

Proton posttranslational modification, a less recognized process, regulates protein function by altering charge and conformation. This rapid, enzyme-free mechanism fine-tunes cellular activities by targeting specific protein sites within physiological pH.

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A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
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A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

Related Experiment Videos

Last Updated: May 13, 2026

Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations
05:57

Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations

Published on: April 26, 2024

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

Area of Science:

  • Biochemistry and Molecular Biology
  • Cellular Signaling

Background:

  • Posttranslational modifications (PTMs) are crucial for regulating protein function, activity, and stability.
  • Proton modification (protonation/deprotonation) is an evolutionarily conserved PTM, yet less recognized than phosphorylation or ubiquitination.
  • PTMs by protons occur within physiological pH ranges, influencing protein conformation and function by altering amino acid side chain charges.

Purpose of the Study:

  • To explore the structural mechanisms underlying proton posttranslational modification.
  • To investigate the functional consequences of proton PTMs on pH-sensing proteins.
  • To highlight the role of protonation in regulating diverse cellular processes.

Main Methods:

  • Examination of structural mechanisms of proton PTMs.
  • Analysis of functional consequences in pH-sensing proteins.
  • Review of literature on protonation dynamics and protein regulation.

Main Results:

  • Proton PTMs rapidly and reversibly alter protein charge, driving conformational changes.
  • Unlike other PTMs, protonation does not require enzymatic machinery.
  • Specificity is achieved through a minority of sites titrating within physiological pH.

Conclusions:

  • Proton posttranslational modification is a significant, yet underappreciated, regulatory mechanism.
  • This process dynamically influences protein function and cellular signaling.
  • Understanding proton PTMs is key to comprehending cellular regulation in response to pH changes.