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Related Concept Videos

Phosphorylation01:02

Phosphorylation

50.8K
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...
50.8K
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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Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

18.0K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
18.0K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

6.9K
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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Protein Folding01:22

Protein Folding

119.0K
Overview
119.0K
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

8.7K
When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
8.7K

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Related Experiment Video

Updated: Aug 22, 2025

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

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How phosphorylation impacts intrinsically disordered proteins and their function.

Estella A Newcombe1,2,3, Elise Delaforge1,2,3, Rasmus Hartmann-Petersen1,2

  • 1REPIN, Department of Biology, University of Copenhagen, Ole Maaløes vej 5, DK-2200 Copenhagen N, Denmark.

Essays in Biochemistry
|November 9, 2022
PubMed
Summary
This summary is machine-generated.

Phosphorylation, a common protein modification, significantly impacts intrinsically disordered proteins (IDPs). Even single phosphorylations on these flexible proteins can alter function, with multiple sites enabling complex biological mechanisms.

Keywords:
allosteric regulationintrinsically disordered proteinsmolecular mechanismsphosphorylation/dephosphorylationpost translational modificationprotein-protein interactions

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Oligopeptide Competition Assay for Phosphorylation Site Determination

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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Phosphorylation is the most frequent post-translational modification (PTM) in eukaryotes.
  • Intrinsically disordered proteins (IDPs) are highly flexible and dynamic.
  • IDPs frequently undergo phosphorylation, impacting their function.

Purpose of the Study:

  • To explore the fundamental effects of phosphorylation on intrinsically disordered proteins (IDPs).
  • To discuss how multisite phosphorylation of IDPs reveals complex biological mechanisms.
  • To provide perspectives on IDP phosphorylation in disease and its interplay with other PTMs.

Main Methods:

  • Review of existing literature on protein phosphorylation and IDPs.
  • Analysis of case studies involving multisite phosphorylation of IDPs.
  • Discussion of the functional consequences of phosphorylation on IDP conformational ensembles.

Main Results:

  • A single phosphoryl group can dramatically alter IDP function.
  • Multiple phosphorylation sites on IDPs increase functional complexity and enable novel mechanisms.
  • Understanding IDP phosphorylation is crucial for deciphering complex biological outputs.

Conclusions:

  • The impact of phosphorylation on IDPs is diverse and complex, despite the chemical simplicity of the modification.
  • Multisite phosphorylation of IDPs broadens our understanding of PTMs.
  • Further research into IDP phosphorylation is vital for understanding disease and other PTM interactions.