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Related Concept Videos

Protein Folding01:25

Protein Folding

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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.
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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.
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Amyloid Fibrils03:03

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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. 
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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.
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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
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Strain phenomenon in protein aggregation: Interplay between sequence and conformation.

Leonid Breydo1

  • 1Department of Molecular Medicine; Morsani College of Medicine; University of South Florida; Tampa, FL USA.

Intrinsically Disordered Proteins
|May 19, 2017
PubMed
Summary
This summary is machine-generated.

Protein aggregates, known as prions, can adopt distinct, heritable conformations called strains. These amyloid strains exhibit varied properties and can even transmit characteristics between different protein sequences.

Keywords:
amyloidprionprotein aggregationseedingstrains

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • Prions and amyloid fibrils exist in diverse, stable conformations (strains).
  • These conformational states possess distinct physical and biological characteristics.
  • Strain properties influence disease pathology and incubation times in mammalian prion diseases.

Purpose of the Study:

  • To explore the generalizability of the prion strain phenomenon beyond prion proteins.
  • To investigate the in vitro and in vivo propagation of distinct amyloid conformational states.
  • To determine if strain characteristics can be transmitted between unrelated protein sequences.

Main Methods:

  • Studies of yeast and mammalian prions.
  • Propagation of amyloid fibrils and oligomers in vitro and in vivo.
  • Analysis of conformational stability and biological properties.

Main Results:

  • Distinct conformational states (strains) of protein aggregates are propagable.
  • Amyloid strain properties are conserved across different protein sequences.
  • Strain characteristics can be transmitted between unrelated sequences.

Conclusions:

  • The strain phenomenon is a general feature of protein aggregation.
  • Amyloid strains represent a fundamental mechanism in protein misfolding diseases.
  • Understanding strain transmission is crucial for developing therapeutic strategies.