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Structural characterization of p53 isoforms due to the polymorphism at codon 72 by mass spectrometry and circular dichroism
Authors:Marina Naldi  Marco Pistolozzi  Carlo Bertucci  Angela De Simone  Serena Altilia  Michela Pierini  Claudio Franceschi  Stefano Salvioli  Vincenza Andrisano
Affiliation:1. Department of Pharmaceutical Sciences, via Belmeloro 6, 40126 Bologna, Italy;2. Department of Experimental Pathology, via S. Giacomo 12, 40126 Bologna, Italy;3. Interdepartmental Centre “L. Galvani” (C.I.G.), Via Selmi 3, 40126 Bologna, Italy
Abstract:A common polymorphism at codon 72 of human TP53 gene determines a proline to arginine aminoacidic substitution within the proline-rich domain of p53 protein. The two resulting isoforms (p53P72 and p53R72) are different from a biochemical and biological point of view and many reports suggest that they can modulate individual cancer susceptibility and overall survival. In the attempt to explain the observed biological differences, we characterized the two isoforms by mass spectrometry and circular dichroism (CD) to evaluate the possible alteration in the secondary structure of p53 introduced by this polymorphism.
Keywords:p53 Isoforms p53P72 and p53R72   Primary and secondary structure characterizations   LC&ndash  ESI-QTOF   LC&ndash  ESI-IT   MALDI-TOF   Tryptic digest   Circular dichroism
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