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Determination Of Protein Content In Materials And Analysis To Motif Of Protein Structure

Posted on:2007-06-04Degree:MasterType:Thesis
Country:ChinaCandidate:Y F WangFull Text:PDF
GTID:2121360212499172Subject:Applied Chemistry
Abstract/Summary:PDF Full Text Request
Determination of protein content plays an important role in the protein imprinting technology. Traditionally, the determination of protein content was performed in aqueous solution. Content of protein within crosslinked polymer was frequently measured by using the radioactive isotope tracer method. In the paper, we develop a simple approach for determination of content of protein in solid materials. i.e. the first attempts made to combine the three approaches, by carrying out biuret reaction (copper complex), cinerating polymer at high temperature (decomposition) and then measuring atomic absorption spectrum (determination of copper content), leading to data showing protein content within crosslinked polymers trapping protein molecule.On the other hand, it is widely believed that a major factor in maintaining the specific structures and performing the biological functions of native proteins is the tendency of several amino acid residues to pack together in the interior of the protein molecule. Here, analyzing the spatial arrangement of residues in protein structure, we recognized the plyads of 2?5 residues, and computed the occurrence frequencies and the frequency distributions. Results shows that the diad between two residues is of paramount importance in packing protein conformation. Triad, tetrad and pentad of residues are closely related to biological role of the protein, providing a useful basis for understanding the relationship between protein structures and their functions.
Keywords/Search Tags:Protein content, trapping of protein by polymer, copper complex, cineration, assembly of amino acid residues, catalytic triad, active site
PDF Full Text Request
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