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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...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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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Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
05:58

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

Intrinsic disorder modulates protein self-assembly and aggregation.

Alfonso De Simone1, Craig Kitchen, Ann H Kwan

  • 1Division of Molecular Biosciences, Imperial College London, South Kensington SW7 2AZ, United Kingdom.

Proceedings of the National Academy of Sciences of the United States of America
|April 18, 2012
PubMed
Summary

Flexible protein regions influence aggregation. Highly dynamic areas, driven by unfavorable entropy, are key to protein solubility and functional states, impacting amyloid formation.

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Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
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Area of Science:

  • Structural biology
  • Biophysics
  • Computational biology

Background:

  • Proteins typically exist in soluble, functional states under physiological conditions.
  • Protein self-assembly into amyloid fibrils is often pathological but can be functional.
  • Fungal hydrophobins exemplify functional amyloids, aiding spore dispersal via air-water interface aggregation.

Purpose of the Study:

  • To investigate the molecular factors determining functional amyloid formation in class I fungal hydrophobin EAS.
  • To differentiate between aggregation-prone and soluble states of EAS using multiscale simulations.

Main Methods:

  • Employed extensive sampling via full-atom replica-exchange molecular dynamics simulations.
  • Utilized coarse-grained simulations to analyze protein aggregation determinants.
  • Investigated the influence of protein dynamics and entropic terms on aggregation propensity.

Main Results:

  • Identified specific factors distinguishing aggregation-prone from soluble EAS states.
  • Demonstrated that unfavorable entropic terms in highly dynamical regions critically influence aggregation propensity.
  • Highlighted the crucial role of flexible structural elements in maintaining protein solubility.

Conclusions:

  • Flexible protein regions are vital for maintaining soluble and functional protein states.
  • Understanding these dynamics is key to comprehending both physiological protein behavior and pathological amyloid formation.
  • Findings provide generalizable insights into protein stability and self-assembly mechanisms.