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Related Concept Videos

Protein Organization01:13

Protein Organization

Overview
Protein Folding01:22

Protein Folding

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Protein Folding01:22

Protein Folding

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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.
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Protein Folding01:25

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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.
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...

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Updated: May 9, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

A surprising simplicity to protein folding.

D Baker1

  • 1Department of Biochemistry, University of Washington, Seattle 98195, USA.

Nature
|May 16, 2000
PubMed
Summary

Protein folding complexity is simplified by fundamental physics. Folding rates and mechanisms are determined by the native state

Area of Science:

  • Biochemistry and Biophysics
  • Computational Biology

Background:

  • Proteins are complex molecules with millions of potential atomic interactions.
  • Predicting protein structure and folding mechanisms is challenging due to this complexity.

Purpose of the Study:

  • To investigate the fundamental physics governing protein folding.
  • To explore new methods for predicting protein structure and folding mechanisms.

Main Methods:

  • Analysis of the fundamental physics underlying protein folding.
  • Development and application of novel predictive methods.

Main Results:

  • Protein folding rates and mechanisms are primarily dictated by the topology of the native state.
  • New methods demonstrate significant promise in predicting protein folding and structure.

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OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

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Related Experiment Videos

Last Updated: May 9, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

Conclusions:

  • The underlying physics of protein folding may be simpler than anticipated.
  • Predictive modeling of protein structure and folding mechanisms is becoming increasingly feasible.