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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...
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...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...

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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

Comparing proteins by their unfolding pattern.

Elias M Puchner1, Gereon Franzen, Mathias Gautel

  • 1Lehrstuhl für Angewandte Physik and Center for Nanoscience, LMU München, Munich, Germany. elias.puchner@physik.lmu.de

Biophysical Journal
|June 14, 2008
PubMed
Summary
This summary is machine-generated.

This study introduces contour length as a superior variable to extension for analyzing single-molecule force spectroscopy data. This method provides accurate energy barrier measurements, enabling better comparison and analysis of biomolecular unfolding events.

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Last Updated: Jul 4, 2026

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Published on: July 16, 2017

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Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Area of Science:

  • Biophysics
  • Biochemistry
  • Molecular Biology

Background:

  • Single-molecule force spectroscopy (SMFS) is crucial for studying biomolecular folding potentials.
  • SMFS records unfolding events as force-extension traces, but these are prone to fluctuations.
  • Current methods struggle with analyzing large protein populations due to inherent variability.

Purpose of the Study:

  • To address limitations of force-extension traces in SMFS analysis.
  • To establish contour length as a more robust variable for quantifying unfolding energy barriers.
  • To develop an improved method for analyzing and comparing biomolecular unfolding data.

Main Methods:

  • Developed a transformation of force-extension traces into contour length space.
  • Generated barrier position histograms from contour length data.
  • Averaged and cross-superimposed histograms to analyze unfolding potentials and event order.

Main Results:

  • Contour length is independent of fluctuations and experimental parameters, offering a more accurate representation of energy barriers.
  • Barrier position histograms reveal and allow averaging of unfolding energy barriers.
  • Demonstrated independent unfolding steps in titin kinase, contrasting with sequential unfolding in bacteriorhodopsin.

Conclusions:

  • Contour length analysis significantly enhances the accuracy of SMFS data interpretation.
  • The developed method facilitates detailed investigation of unfolding potentials and the order of events.
  • This approach enables automated analysis and screening of force spectroscopy data for various proteins.