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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
Protein Organization01:13

Protein Organization

Overview
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Denaturation01:28

Protein Denaturation

The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...

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Related Experiment Video

Updated: Jun 22, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Computing protein stabilities from their chain lengths.

Kingshuk Ghosh1, Ken A Dill

  • 1Department of Physics, University of Denver, Denver, CO 80209, USA. kghosh@du.edu

Proceedings of the National Academy of Sciences of the United States of America
|June 23, 2009
PubMed
Summary
This summary is machine-generated.

Researchers can now predict protein stability and folding properties using only basic genomic data like chain length and charged side chain count. This bioinformatics advance allows for efficient, large-scale annotation of proteomes with crucial stability information.

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Last Updated: Jun 22, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

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Published on: July 14, 2015

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Published on: November 3, 2011

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:

  • Biophysics
  • Bioinformatics
  • Genomics

Background:

  • Modern genomics rapidly generates new protein sequences.
  • Bioinformatics methods often infer protein structure and function.
  • Protein stability and folding properties are critical but less frequently predicted.

Purpose of the Study:

  • To demonstrate the prediction of protein stability and thermal folding properties from simple genomic information.
  • To develop an analytical model for inferring thermodynamic parameters and phase equilibria.

Main Methods:

  • Utilizing protein chain length and charged side chain counts as input.
  • Developing an analytical model to predict folding enthalpy, entropy, heat capacity, and free energy as functions of temperature.
  • Calculating denaturant m values, pH-temperature-salt phase diagrams, and confinement energy.

Main Results:

  • The model successfully predicts key thermodynamic parameters (DeltaH(T), DeltaS(T), DeltaC(p), DeltaF(T)) and phase equilibria.
  • Demonstrated computation of conditions (pH, salt) for protein denaturation in confined spaces.
  • The analytical nature of the model ensures computational efficiency.

Conclusions:

  • Protein stability and folding characteristics can be inferred from basic genomic data.
  • The model offers a computationally efficient method for predicting diverse protein properties.
  • Enables automated annotation of entire proteomes with protein stability information.