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Related Concept Videos

ATP Synthase: Structure01:18

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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...
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
RNA Polymerase II Accessory Proteins02:36

RNA Polymerase II Accessory Proteins

Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...
RNA Polymerase II Accessory Proteins02:36

RNA Polymerase II Accessory Proteins

Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

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Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions
11:22

Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions

Published on: January 30, 2018

Flexibility in the PP1:spinophilin holoenzyme.

Michael J Ragusa1, Marc Allaire, Angus C Nairn

  • 1Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI, USA.

FEBS Letters
|November 25, 2010
PubMed
Summary
This summary is machine-generated.

Protein phosphatase 1 (PP1) holoenzymes remain dynamic after formation. This flexibility in the PP1:spinophilin complex enhances spinophilin

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Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels
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Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels

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Last Updated: Jun 6, 2026

Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions
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Published on: January 30, 2018

Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels
11:19

Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels

Published on: July 4, 2016

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Protein phosphatase 1 (PP1) is a key enzyme regulated by approximately 200 interacting proteins, forming holoenzymes.
  • These holoenzymes direct PP1 activity and localization, but the flexibility of formed holoenzymes is not well understood.
  • PP1 regulatory proteins exhibit known dynamics in their unbound states.

Purpose of the Study:

  • To investigate the solution structure and flexibility of the Protein phosphatase 1:spinophilin (PP1:spinophilin) holoenzyme.
  • To understand how holoenzyme formation affects the inherent dynamics of PP1 regulatory proteins.

Main Methods:

  • Small-angle X-ray scattering (SAXS) was employed to study the PP1:spinophilin holoenzyme in solution.
  • SAXS data provided insights into the overall structure and flexibility of the complex.

Main Results:

  • The PP1:spinophilin holoenzyme exhibits significant dynamic behavior in solution.
  • This residual flexibility increases the effective capture radius of spinophilin.
  • The observed dynamics are likely crucial for the biological function of the holoenzyme.

Conclusions:

  • Holoenzyme formation does not eliminate the inherent flexibility of PP1 regulatory proteins like spinophilin.
  • The dynamic nature of the PP1:spinophilin holoenzyme is essential for its function, potentially by facilitating interactions.
  • Further studies can explore the implications of this flexibility in various cellular contexts.