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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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Related Experiment Video

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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
10:09

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Published on: April 28, 2011

Understanding the folding-function tradeoff in proteins.

Shachi Gosavi1

  • 1National Centre for Biological Sciences, Tata Institute of Fundamental Research, Bangalore, India. shachi@ncbs.res.in

Plos One
|April 18, 2013
PubMed
Summary

Protein folding can be compromised for function. We developed a method to isolate protein folding motifs, revealing how function impacts folding speed and stability, aiding in protein design.

Area of Science:

  • Biophysics
  • Structural Biology
  • Computational Biology

Background:

  • Protein sequence optimization often involves a trade-off between folding stability and biological function.
  • Understanding how functional adaptations influence protein folding is crucial for predicting protein behavior and designing novel proteins.

Purpose of the Study:

  • To develop a novel method for extracting protein folding motifs, independent of function.
  • To investigate the impact of functional sites on the folding process of the β-trefoil fold.
  • To explore the utility of folding motifs in functional annotation and protein design.

Main Methods:

  • Developed a computational method to extract 'function-less' folding motifs from structurally similar proteins with diverse functions.
  • Utilized structure-based models and molecular dynamics simulations to study the folding of the β-trefoil folding motif.

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Microfluidic Mixers for Studying Protein Folding

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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

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

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  • Compared the folding dynamics of the motif with wild-type β-trefoil proteins (interleukin-1β and hisactophilin).

    • Main Results:

    • Identified the β-trefoil folding motif and analyzed its folding properties.
    • Demonstrated that functional sites can increase folding complexity and slow down folding (e.g., interleukin-1β).
    • Showed that functional residue usage can decrease native contact density and accelerate folding (e.g., hisactophilin).

    Conclusions:

    • Protein function significantly influences folding kinetics and pathways.
    • The extracted folding motif serves as a valuable tool for identifying subtle structural variations affecting folding.
    • Folding motifs can aid in functional annotation and provide a basis for designing novel scaffold proteins with engineered functions.