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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...
Protein Folding01:22

Protein Folding

Overview
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...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

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Related Experiment Video

Updated: Jun 13, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Multiscale methods for protein folding simulations.

Wenfei Li1, Hiroaki Yoshii, Naoto Hori

  • 1Department of Biophysics, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan.

Methods (San Diego, Calif.)
|May 4, 2010
PubMed
Summary
This summary is machine-generated.

Multiscale computational methods enhance protein folding studies by combining atomistic and coarse-grained simulations for improved accuracy and efficiency. This review details current protocols, applications, and future directions for these powerful protein dynamics tools.

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Last Updated: Jun 13, 2026

Microfluidic Mixers for Studying Protein Folding
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Published on: April 10, 2012

Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion
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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

Area of Science:

  • Computational Biology
  • Biophysics
  • Biochemistry

Background:

  • Proteins exhibit inherent hierarchical structures, necessitating advanced computational approaches for studying their dynamics.
  • Traditional simulation methods face limitations in accurately and efficiently capturing the full spectrum of protein functional dynamics.

Purpose of the Study:

  • To provide a comprehensive overview of multiscale computational methods for protein dynamics.
  • To detail current multiscale protocols and their applications in protein folding simulations.
  • To discuss the advantages, limitations, and scope of various multiscale strategies.

Main Methods:

  • Coupling of atomistic and coarse-grained simulation techniques.
  • Development and implementation of diverse multiscale protocols tailored to specific research questions.
  • Application of multiscale methods to protein folding simulations.

Main Results:

  • Demonstration of enhanced accuracy and efficiency in protein dynamics studies through multiscale simulations.
  • Comparative analysis of different multiscale protocols, highlighting their respective strengths and weaknesses.
  • Successful application of multiscale strategies in simulating protein folding processes.

Conclusions:

  • Multiscale computational methods are essential for understanding complex protein folding and functional dynamics.
  • The choice of multiscale protocol significantly impacts simulation outcomes and efficiency.
  • Future developments should focus on refining existing protocols and exploring novel multiscale approaches for broader applicability.