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Protein Folding

Protein Folding

Protein Folding

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 Folding

Protein Folding

Protein and Protein Structure

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...

Protein Organization

Protein Organization

Protein Organization

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.

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Related Experiment Video

Updated: Jun 20, 2026

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen

Published on: March 4, 2017

Shape and evolution of thermostable protein structure.

Ryan G Coleman¹, Kim A Sharp

¹The Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.

|September 5, 2009

Summary

Organisms thriving at high temperatures possess more spherical proteins with deeper atomic burial and shallower surface pockets compared to their mesostable counterparts. This structural adaptation enhances protein stability in extreme thermal environments.

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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

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Last Updated: Jun 20, 2026

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen

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

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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

Area of Science:

Structural Biology
Biophysics
Evolutionary Biology

Background:

Organisms at high temperatures require robust protein structures resistant to thermal denaturation.
Protein structure differences arise from adaptations to varying thermal environments.

Purpose of the Study:

To investigate geometric differences in thermostable versus mesostable proteins.
To understand the structural constraints on proteins from thermophilic organisms.

Main Methods:

Analysis of thermostable/mesostable homologous protein structures.
Application of geometric measures: burial depth, travel depth, packing, and Wadell Sphericity.
Residue-level analysis of atomic burial depth.

Main Results:

Hyperthermostable proteins exhibit significantly lower mean travel depth, indicating fewer and shallower surface pockets.
Hyperthermostable proteins show significantly higher mean burial depth, with more atoms buried deeper.
Hyperthermostable proteins are demonstrably more spherical than mesostable homologues.
Residue-specific analysis reveals charged residues remain unburied, while other residues, particularly Alanine, are more buried in hyperthermostable proteins.

Conclusions:

Thermostable proteins adopt a more compact and spherical structure with optimized surface topography.
Atomic burial depth and surface pocket geometry are key adaptations for protein stability at high temperatures.
These findings provide novel insights into the molecular mechanisms of thermoadaptation.