Next Article in Journal
Long Noncoding Competing Endogenous RNA Networks in Age-Associated Cardiovascular Diseases
Next Article in Special Issue
bHLH–PAS Proteins: Their Structure and Intrinsic Disorder
Previous Article in Journal
Role of Hedgehog Signaling in Vasculature Development, Differentiation, and Maintenance
Previous Article in Special Issue
Repeats in S1 Proteins: Flexibility and Tendency for Intrinsic Disorder
Open AccessArticle

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

Biophysics & Nanoscience Centre, DEB, Università della Tuscia, 01100 Viterbo, Italy
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2019, 20(12), 3078; https://doi.org/10.3390/ijms20123078
Received: 15 May 2019 / Revised: 13 June 2019 / Accepted: 20 June 2019 / Published: 24 June 2019
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 α-helix, β-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. View Full-Text
Keywords: Raman spectroscopy; p53; intrinsically disordered protein; blue copper protein Azurin; protein–protein interaction; Amide I band deconvolution; principal component analysis Raman spectroscopy; p53; intrinsically disordered protein; blue copper protein Azurin; protein–protein interaction; Amide I band deconvolution; principal component analysis
Show Figures

Figure 1

MDPI and ACS Style

Signorelli, S.; Cannistraro, S.; Bizzarri, A.R. Raman Evidence of p53-DBD Disorder Decrease upon Interaction with the Anticancer Protein Azurin. Int. J. Mol. Sci. 2019, 20, 3078.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop