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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 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...
Protein Folding01:22

Protein Folding

Overview
Protein Denaturation01:28

Protein Denaturation

The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...

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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
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Influence of sequence changes and environment on intrinsically disordered proteins.

Amrita Mohan1, Vladimir N Uversky, Predrag Radivojac

  • 1School of Informatics and Computing, Indiana University, Bloomington, Indiana, United States of America.

Plos Computational Biology
|September 5, 2009
PubMed
Summary

Intrinsically disordered protein regions vary significantly in X-ray structures due to sequence changes and experimental conditions, challenging static model assumptions. This highlights the dynamic nature of protein disorder and its environmental regulation.

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Related Experiment Videos

Last Updated: Jun 20, 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

Estimation of Structural Sensitivity of Intrinsically Disordered Regions in Response to Hyperosmotic Stress in Living Cells Using FRET
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Estimation of Structural Sensitivity of Intrinsically Disordered Regions in Response to Hyperosmotic Stress in Living Cells Using FRET

Published on: January 12, 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:

  • Structural Biology
  • Biochemistry
  • Protein Science

Background:

  • Large-scale protein studies often rely on static models from the Protein Data Bank.
  • Static models offer limited insight into protein structure and function variations under different conditions.
  • The robustness of intrinsically disordered regions (IDRs) to sequence or environmental changes is not well understood.

Purpose of the Study:

  • To investigate the sensitivity of intrinsically disordered regions to variations in protein sequence and crystallographic experimental parameters.
  • To assess the impact of these variations on the observed structural characteristics of IDRs.

Main Methods:

  • Analysis of intrinsically disordered regions in homologous proteins crystallized independently.
  • Systematic study of IDR behavior under altered protein sequences and crystallographic conditions.

Main Results:

  • Observed significant changes in the existence, position, and length of intrinsically disordered regions.
  • Demonstrated that the appearance of IDRs in X-ray structures is highly dependent on amino acid sequence.
  • Highlighted the influence of specific crystallographic experiment parameters on IDR manifestation.

Conclusions:

  • The structural representation of intrinsically disordered regions in X-ray crystallography is highly variable.
  • Protein disorder is sensitive to both sequence context and experimental conditions.
  • Raises fundamental questions about protein evolution and the regulation of protein dynamics and function by environmental factors.