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An Analysis Of Protein Folding Structure And Folding Rate Prediction

Posted on:2017-05-23Degree:MasterType:Thesis
Country:ChinaCandidate:Q FanFull Text:PDF
GTID:2370330488463845Subject:Optics
Abstract/Summary:PDF Full Text Request
Protein is the most common material existed in living things and plays an important role in all of their activities.Protein folding problem is one of the key tasks in biophysics.It mainly studies the relationship of the protein sequence,structure and function.Protein folding focuses on two directions:the relationship between the structure and sequence,and the relationship among the sequence,structure and folding rate.1.Fluorescence spectrometry technology plays an important part in the study of protein folding and its quantitative analysis.This chapter discusses the concept of fluorescence spectrometry,luminescence mechanism and characteristics of fluorescence spectrometry,and analyzes the fluorescence spectroscopy research mechanism of protein folding,and discusses the application of in the detection of protein conformation change,and protein content and the characteristics.2.Based on the 2D HP model simulating the process of protein folding using the Monte Carlo algorithm by computer.Using five different classification methods based on hydrophobic of amino acid analyzes the effect on the protein folding and minimum energy.The simulation experimental results of 2D HP show that for the division of different hydrophobic of amino acids has a great influence on the minimum energy in testing the sequence of proteins;In the same sequence for one hydrophobic method,Starting from the different direction of protein folding structure,reverse sequences find same results.There is a certain relationship between protein folding structure and energy.3.Protein folding rate is predicted by hydrophobic value of 20 amino acids based on sequence and analyzed the influence of hydrophobic.Research Results show that hydrophobic in 20 amino acids for one of the crucial factors that affect of protein folding rate.4.The chapter extract Ca and N form the main chains and the first carbon atoms of side chain Cb from the tertiary structures of proteins,using the characteristics of protein atom contact number analysis the effect of the protein folding rate by regression analysis.It draws a conclusion that the Ca contact number predict folding rate better than with Cb and N contact number predicted results?...
Keywords/Search Tags:Protein folding, Folding model, Folding rate, Hydrophobic of amino acids, Protein structural classes, Regression analysis, Contact number
PDF Full Text Request
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