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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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Protein Kinases and Phosphatases02:54

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¹H NMR: Complex Splitting01:13

¹H NMR: Complex Splitting

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A proton M that is coupled to a proton X results in doublet signals for M. However, NMR-active nuclei can be simultaneously coupled to more than one nonequivalent nucleus. When M is coupled to a second proton A, such as in styrene oxide, each peak in the doublet is split into another doublet.
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¹H NMR Signal Multiplicity: Splitting Patterns01:13

¹H NMR Signal Multiplicity: Splitting Patterns

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When protons A and X are coupled, their nuclear spin energy levels are slightly modified. This is because the energy required to excite proton A to a spin state parallel to proton X is slightly different from the energy required for it to become anti-parallel to spin X. Consequently, there are two possible excitation frequencies for A (A1 and A2), depending on the spin state of X, and vice versa. The mutual nature of coupling implies that the difference between frequencies A1 and A2, indicated...
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IR Spectrum Peak Splitting: Symmetric vs Asymmetric Vibrations01:08

IR Spectrum Peak Splitting: Symmetric vs Asymmetric Vibrations

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Identical bonds within a polyatomic group can stretch symmetrically (in-phase) or asymmetrically (out-of-phase). Similar to hydrogen bonding, these vibrations also influence the shape of the IR peak. Generally, asymmetric stretching frequencies are higher than symmetric stretching frequencies. For example, primary amines exhibit two distinct IR peaks between 3300–3500 cm−1 corresponding to the symmetric and asymmetric N-H stretching, while secondary amines exhibit a single...
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Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule01:10

Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule

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In the AX proton spin system, proton A can sense the two spin states of a coupled proton X, resulting in a doublet NMR signal with two peaks of equal (1:1) intensity. When proton A is coupled to two equivalent protons (AX2 spin system), the spin states of each X can be aligned with or against the external field, creating three possible scenarios. This results in a 1:2:1  triplet signal, where the central peak corresponds to the chemical shift of A and is twice as large or intense as the...
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Updated: Feb 1, 2026

Direct Detection of Isolevuglandins in Tissues Using a D11 scFv-Alkaline Phosphatase Fusion Protein and Immunofluorescence
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The split protein phosphatase system.

Anne Bertolotti1

  • 1MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, U.K. aberto@mrc-lmb.cam.ac.uk.

The Biochemical Journal
|December 8, 2018
PubMed
Summary
This summary is machine-generated.

Protein Phosphatase 1 (PP1) enzymes, crucial for cellular processes, achieve selectivity through a split system. This involves a catalytic subunit and a non-catalytic substrate receptor subunit working together.

Keywords:
biochemical techniques and resourcesintracellular signalingprotein phosphatases

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Reversible protein phosphorylation regulates cellular functions via kinases and phosphatases.
  • Protein kinases are well-studied, while protein phosphatases remain relatively neglected.
  • Protein Phosphatase 1 (PP1) dephosphorylates many phospho-serines and phospho-threonines, controlling diverse cellular processes.

Purpose of the Study:

  • To review the discovery and evolving understanding of protein phosphatases.
  • To highlight the exquisite selectivity of PP1 phosphatases, challenging previous views of unselectivity.
  • To propose a model for PP1 selectivity based on the interaction of catalytic and non-catalytic subunits.

Main Methods:

  • Review of existing literature on protein phosphatases.
  • In-depth analysis of two specific holophosphatases.
  • Conceptual model development based on experimental findings.

Main Results:

  • PP1 phosphatases are obligatory heteromers, unlike kinases.
  • Selectivity arises from the assembly of catalytic and non-catalytic subunits, the latter acting as a substrate receptor.
  • PP1 and its substrate receptors form a 'split protein phosphatase system'.

Conclusions:

  • The non-catalytic subunit is essential for PP1 holoenzyme function and substrate specificity.
  • The 'split enzyme' model explains how PP1 achieves selective dephosphorylation.
  • This framework may aid in studying poorly understood phosphatases and identifying their substrates.