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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...
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...
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...
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...
Protein Folding01:22

Protein Folding

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Related Experiment Video

Updated: May 29, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

Intrinsically disordered proteins as molecular shields.

Sohini Chakrabortee1, Rashmi Tripathi, Matthew Watson

  • 1Department of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, UK.

Molecular Biosystems
|September 13, 2011
PubMed
Summary
This summary is machine-generated.

LEA proteins act as molecular shields, preventing protein aggregation during desiccation, unlike classical molecular chaperones like HSP70. This distinct function protects cellular proteomes from drying-induced damage.

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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

Related Experiment Videos

Last Updated: May 29, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Folding

Background:

  • Late Embryogenesis Abundant (LEA) proteins are intrinsically disordered proteins (IDPs) implicated in desiccation tolerance.
  • A key proposed function of LEA proteins is to prevent protein aggregation during dehydration (anhydrobiosis).

Purpose of the Study:

  • To differentiate the anti-aggregation activity of LEA proteins from classical molecular chaperones.
  • To elucidate the mechanism of LEA protein-mediated protection against desiccation-induced damage.

Main Methods:

  • Comparative analysis of LEA proteins (AavLEA1, Em) and HSP70 in preventing protein aggregation under heat and desiccation stress.
  • Förster resonance energy transfer (FRET) to study protein interactions.
  • Assessment of intramolecular damage using monomeric red fluorescent protein (mCherry).
  • Bioinformatics survey of protein disorder in desiccation-tolerant versus intolerant species.

Main Results:

  • LEA proteins protect against desiccation-induced protein aggregation, while HSP70 does not.
  • HSP70, but not LEA proteins, prevents heat-induced aggregation of citrate synthase.
  • LEA proteins exhibit loose interactions with client proteins, distinct from the tight binding of HSP70.
  • Synthetic polysaccharides mimic LEA protein's anti-aggregation activity, supporting a steric interference model.
  • LEA proteins do not prevent intramolecular damage to mCherry, indicating a primarily intermolecular protective role.
  • Bioinformatics analysis found no significant difference in intrinsic disorder between tolerant and intolerant species.

Conclusions:

  • LEA proteins function as molecular shields, distinct from molecular chaperones, primarily through intermolecular interactions to prevent protein aggregation during desiccation.
  • This molecular shield function is crucial for proteostasis in anhydrobiotic organisms.
  • The intrinsic disorder hypothesis for desiccation tolerance is not supported by the data.