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Related Concept Videos

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...
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...
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 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

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Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
11:04

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Published on: June 23, 2018

A statistical mechanical approach to protein aggregation.

John S Schreck1, Jian-Min Yuan

  • 1Department of Physics, Drexel University, Philadelphia, Pennsylvania 19104, USA. jss74@drexel.edu

The Journal of Chemical Physics
|December 24, 2011
PubMed
Summary
This summary is machine-generated.

We developed a statistical mechanics model for protein aggregation, crucial for understanding neurodegenerative diseases and designing biomaterials. Our theory accurately predicts aggregation behavior, including nucleation and phase diagrams, aligning with experimental data.

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Area of Science:

  • Statistical mechanics
  • Biophysics
  • Materials science

Background:

  • Protein aggregation is implicated in neurodegenerative diseases and has potential applications in biomaterials.
  • Understanding the complex self-assembly of peptides and proteins is crucial for both therapeutic and material development.

Purpose of the Study:

  • To develop a theoretical framework for protein aggregation using statistical mechanical methods.
  • To model complex aggregation systems, including peptide/protein self-assembly, with multiple structural levels.

Main Methods:

  • Developed an effective Hamiltonian considering interactions between protein monomers, solvent, and filaments.
  • Utilized a Zimm-Bragg-like transfer matrix for exact calculation of the grand partition function.
  • Employed Potts models (q-states) for protein monomer descriptions on n x N lattices.

Main Results:

  • Obtained exact solutions for thermodynamic properties.
  • Characterized nucleation processes and generated phase diagrams.
  • Quantified aggregate sheet content as a function of protein number and interaction energies.

Conclusions:

  • The developed statistical mechanics model provides accurate predictions for protein aggregation.
  • The model successfully applied to Aβ(1-40) and Curli fibrils, showing good agreement with experimental findings.
  • This approach offers a powerful tool for studying protein self-assembly and designing novel biomaterials.