Related Experiment Video
Updated: May 20, 2026
10:09
Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
Published on: April 28, 2011
Protein photo-folding and quantum folding theory
1Faculty of Physical Science and Technology, Inner Mongolia University, Hohhot 010021, China. lolfcm@mail.imu.edu.cn
Science China. Life Sciences
|June 30, 2012
Summary
This study introduces quantum folding theory to explain how proteins fold with light. A common factor, TAOI, links protein folding and photo-folding, revealing quantum tunneling in protein dynamics.
Area of Science:
- Biophysics
- Quantum Chemistry
- Protein Dynamics
Background:
- Protein folding is crucial for biological function.
- Understanding protein folding mechanisms, especially under external influences like photons, is essential.
- Existing models often do not fully capture the quantum aspects of protein dynamics.
Purpose of the Study:
- To calculate protein folding rates influenced by photon absorption/emission.
- To determine the cross-section of photon-protein inelastic scattering.
- To compare radiative and non-radiative protein folding processes.
Main Methods:
- Utilizing quantum folding theory and a field-theoretical method.
- Calculating rates of protein photo-folding (with photon interaction).
- Comparing these rates with non-radiative folding (without photon interaction).
Main Results:
- A common factor, thermo-averaged overlap integral of the vibration wave function (TAOI), identified for both folding types.
- Predicted identical temperature dependence for stimulated photo-folding rates and photon-protein resonance Raman scattering sections as protein folding.
- Observed broadening of electronic transition spectral lines into bands with reduced vibration spectral line widths.
Conclusions:
- The findings imply quantum tunneling between protein conformations during folding and photo-folding.
- The study demonstrates the quantum nature of the conformational-electronic system's motion.
- TAOI serves as a key factor linking radiative and non-radiative protein folding pathways.
Related Concept Videos
01:25Protein 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 Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
01:22Protein Folding
Overview
01:22Protein Folding
Overview
03:00Molecular 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...
The...
03:00Molecular 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...
The...
03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...