Raman Evidence of p53-DBD Disorder Decrease upon Interaction with the Anticancer Protein Azurin
| Autor: | Anna Rita Bizzarri, Salvatore Cannistraro, Sara Signorelli |
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| Rok vydání: | 2019 |
| Předmět: |
Models
Molecular p53 0301 basic medicine Conformational change principal component analysis Molecular Conformation Spectrum Analysis Raman Intrinsically disordered proteins Article Catalysis Protein–protein interaction lcsh:Chemistry Inorganic Chemistry 03 medical and health sciences symbols.namesake 0302 clinical medicine Azurin Side chain Humans Protein Interaction Domains and Motifs Physical and Theoretical Chemistry lcsh:QH301-705.5 Molecular Biology Protein secondary structure Spectroscopy Binding Sites blue copper protein Azurin Chemistry Organic Chemistry DNA General Medicine intrinsically disordered protein Random coil Computer Science Applications protein–protein interaction 030104 developmental biology lcsh:Biology (General) lcsh:QD1-999 030220 oncology & carcinogenesis Raman spectroscopy Biophysics symbols Tumor Suppressor Protein p53 Protein Binding Amide I band deconvolution |
| Zdroj: | International Journal of Molecular Sciences International Journal of Molecular Sciences, Vol 20, Iss 12, p 3078 (2019) Volume 20 Issue 12 |
| ISSN: | 1422-0067 |
| Popis: | Raman spectroscopy, which is a suitable tool to elucidate the structural properties of intrinsically disordered proteins, was applied to investigate the changes in both the structure and the conformational heterogeneity of the DNA-binding domain (DBD) belonging to the intrinsically disordered protein p53 upon its binding to Azurin, an electron-transfer anticancer protein from Pseudomonas aeruginosa. The Raman spectra of the DBD and Azurin, isolated in solution or forming a complex, were analyzed by a combined analysis based on peak inspection, band convolution, and principal component analysis (PCA). In particular, our attention was focused on the Raman peaks of Tyrosine and Tryptophan residues, which are diagnostic markers of protein side chain environment, and on the Amide I band, of which the deconvolution allows us to extract information about &alpha helix, &beta sheet, and random coil contents. The results show an increase of the secondary structure content of DBD concomitantly with a decrease of its conformational heterogeneity upon its binding to Azurin. These findings suggest an Azurin-induced conformational change of DBD structure with possible implications for p53 functionality. |
| Databáze: | OpenAIRE |
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