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Raman Evidence of p53-DBD Disorder Decrease upon Interaction with the Anticancer Protein Azurin.

Int J Mol Sci. 2019; 
SignorelliSara,CannistraroSalvatore,BizzarriAnna
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摘要

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 . 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 diagnosti... More

关键词

Amide I band deconvolution,Raman spectroscopy,blue copper protein Azurin,intrinsically disordered protein,p53,principal component analysis,protein–protein interac