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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
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...
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...

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Related Experiment Video

Updated: Jul 3, 2026

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
07:22

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project

Published on: February 11, 2019

Bioinformatic method for protein thermal stabilization by structural entropy optimization.

Euiyoung Bae1, Ryan M Bannen, George N Phillips

  • 1Departments of Biochemistry and Computer Science, University of Wisconsin, Madison, WI 53706, USA.

Proceedings of the National Academy of Sciences of the United States of America
|July 16, 2008
PubMed
Summary
This summary is machine-generated.

We developed a new computational method, improved configurational entropy (ICE), to engineer more thermally stable proteins. This approach enhances protein stability and function using only sequence data, showing broad applicability.

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Area of Science:

  • Protein Engineering
  • Computational Biology
  • Biophysics

Background:

  • Enhancing protein thermal stability is crucial for various applications.
  • Current methods often require extensive structural or sequence data.

Purpose of the Study:

  • To develop a novel bioinformatic method for engineering enhanced protein thermal stability.
  • To demonstrate the method's efficacy using adenylate kinase as a model system.

Main Methods:

  • Utilized sequence alignments to optimize local structural entropy.
  • Developed the improved configurational entropy (ICE) method.
  • Applied ICE to redesign a mesophilic adenylate kinase using a single psychrophilic homologue.

Main Results:

  • Designed protein variants with significantly increased thermal stability.
  • Maintained catalytic activity in the engineered proteins.
  • Demonstrated the method's effectiveness without 3D structures or numerous homologous sequences.

Conclusions:

  • The ICE method offers a broadly applicable approach for protein stabilization.
  • Optimizing local structural entropy is key to enhancing protein thermal stability.
  • Entropy plays a critical role in the structural stability of proteins.