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Related Concept Videos

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
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...
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 Organization01:13

Protein Organization

Overview

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Related Experiment Video

Updated: Jun 20, 2026

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
10:50

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

Published on: September 15, 2010

How does a simplified-sequence protein fold?

Enrico Guarnera1, Riccardo Pellarin, Amedeo Caflisch

  • 1Department of Biochemistry, University of Zurich, Zurich, Switzerland.

Biophysical Journal
|September 16, 2009
PubMed
Summary
This summary is machine-generated.

Researchers simplified a protein to study early protein folding. The simplified protein adopted a molten globule state, suggesting evolution optimized amino acids for stable, functional protein structures.

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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

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Related Experiment Videos

Last Updated: Jun 20, 2026

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
10:50

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

Published on: September 15, 2010

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Published on: July 25, 2013

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Folding Dynamics

Background:

  • Investigating primordial protein structures provides insights into early life evolution.
  • The immunoglobulin-binding domain of protein G (56 residues) serves as a model alpha/beta fold.

Purpose of the Study:

  • To explore the folding behavior of a simplified protein sequence.
  • To understand the role of specific amino acid sequences in protein structure and stability.

Main Methods:

  • Sequence simplification of the protein G domain using polyalanine, polythreonine, and diglycine segments.
  • 15-microsecond molecular dynamics simulations at 330 K to observe folding and unfolding events.

Main Results:

  • The simplified protein variant exhibited multiple folding/unfolding events, stabilizing in a molten globule state (20% population) with alpha/beta topology.
  • The unfolded state was heterogeneous, including alpha-helical and beta-sheet structures.
  • Folding to the molten globule state occurred rapidly (<1 microsecond) via a framework mechanism with multiple pathways.

Conclusions:

  • Evolutionary enrichment of amino acids likely optimizes protein function through stabilization of unique structures.
  • Specific tertiary interactions are crucial for stabilizing native protein structures compared to molten globule states.