Article
Version 1
This version is not peer-reviewed
Preliminary Analysis of Protein Catalytic Ability and Catalytic Structure
Version 1
: Received: 17 July 2024 / Approved: 18 July 2024 / Online: 18 July 2024 (16:45:50 CEST)
How to cite: Cao, Z. Preliminary Analysis of Protein Catalytic Ability and Catalytic Structure. Preprints 2024, 2024071526. https://doi.org/10.20944/preprints202407.1526.v1 Cao, Z. Preliminary Analysis of Protein Catalytic Ability and Catalytic Structure. Preprints 2024, 2024071526. https://doi.org/10.20944/preprints202407.1526.v1
Abstract
When water molecules or other particles collide with protein molecules in a solution, the protein molecules absorb some of the momentum and deform, forming a certain molecular potential energy. When a protein molecule in a high-energy state changes to a stable state, if there is a suitable substrate binding and the potential energy of the protein molecule is greater than the energy required to break the substrate chemical bond, catalytic action will occur. The α-helices and β-folds in protein molecules play a major role in converting the kinetic energy of water molecules into their own potential energy due to the large number of amino acids involved and their regular structure. The internal structural deformation of proteins caused by the impact of water molecules on α-helices and β-folds also has a profound impact on the structure of substrates.
Keywords
protein; high-energy state; catalysis; AlphaFold
Subject
Physical Sciences, Biophysics
Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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