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Related Concept Videos

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...
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...
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Organization01:13

Protein Organization

Overview
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

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Related Experiment Video

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

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Published on: September 17, 2017

Alpha proton detection based backbone assignment of intrinsically disordered proteins.

Perttu Permi1, Maarit Hellman

  • 1Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, Helsinki, Finland. Perttu.Permi@helsinki.fi

Methods in Molecular Biology (Clifton, N.J.)
|July 5, 2012
PubMed
Summary

This study introduces a new nuclear magnetic resonance (NMR) assignment protocol using alpha proton detection. This method overcomes limitations of amide proton detection for intrinsically disordered proteins (IDPs) under various conditions.

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

Published on: December 27, 2016

Area of Science:

  • Structural Biology
  • Biophysical Chemistry
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • Accurate assignment of NMR resonance frequencies to specific atoms is fundamental for molecular structural determination.
  • Conventional sequential assignment methods often rely on amide proton detection, which can be problematic for intrinsically disordered proteins (IDPs) at elevated pH or temperatures.

Purpose of the Study:

  • To develop and present an alternative NMR assignment protocol.
  • To overcome the limitations of amide proton-based methods for studying IDPs.
  • To enable sequential assignment of proline-rich segments in IDPs.

Main Methods:

  • Development of an assignment protocol centered on alpha proton detection.
  • Utilizing triple-resonance NMR experiments.
  • Comparison of the new protocol with established amide proton detection methods.

Main Results:

  • The alpha proton-detected triple-resonance experiments offer advantages over amide proton-detected experiments.
  • The developed protocol is effective for studying IDPs across a wide range of pH values.
  • Successful sequential assignment of proline-rich segments was achieved.

Conclusions:

  • The alpha proton-detected NMR assignment protocol provides a robust alternative for structural studies of IDPs.
  • This method enhances the scope of NMR applications for challenging protein targets, including those at high pH and temperature.
  • The protocol facilitates detailed structural insights into IDPs, particularly proline-rich regions.