Method for calculating and calculating inherent polymorphic structure of polymorphic structure disordered protein

Abstract

The invention relates to a method for calculating and calculating a polymorphic structure of inherent disordered protein, and belongs to the field of protein non-equilibrium dynamics and polymorphic structures. Folding or non-equilibrium dynamics simulation is performed on the inherent disordered protein for thousands of times, and important information focusing on structural diagram, clustering and properties of the inherent disordered protein is obtained by statics and analysis. The method comprises the following steps: 1, obtaining a protein experiment structure; 2, calculating a bond angle and a torsion angle formed by central carbon atom links; 3, creating a protein fitting model; 4, simulating a configuration variation process of the inherent disordered protein caused by cellular environment variations; 5, performing heating-cooling simulative cycles on the protein for thousands of times, and determining a low temperature value and a high temperature value of the polymorphic structure; 6, obtaining a purified final state configuration data array; 7, concluding and analyzing the structure cluster of the inherent disordered protein; and 8, visualizing the feature configuration of the structure clustering of the inherent disordered protein. By adoption of the method provided by the invention, the difficulty that the polymorphic structure of the inherent disordered protein cannot be captured at the same time by the traditional theory and the experimental methods at the same time is solved.

Description

technical field [0001] The present invention relates to statistical simulation and analysis of various structural clusters, structural landscapes, structural properties, etc. formed during folding or other non-equilibrium dynamics of inherently disordered proteins, and in particular to a method for statistically calculating polymorphic structures of inherently disordered proteins The method belongs to the field of protein non-equilibrium dynamics and polymorphic structure research. Background technique [0002] Intrinsically disordered protein is a protein that lacks a fixed or ordered three-dimensional spatial structure, and it usually has a series of conformational states ranging from completely unstructured to partially structured (including random coils and molten globules). The traditional paradigm of protein structure-function relationship shows that protein function depends on a fixed three-dimensional spatial structure. However, this is challenged by many findings o...

AI Technical Summary

Problems solved by technology

The folding and dynamic process of many inherently disordered proteins is long and complex, and exploring the structural landscape or clustering of such proteins requires a large number of statistical calculations, which is difficult to achieve with molecular dynamics methods

So far, there are no theoretical methods and results in this area

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