p53 AlphaFold Structure Analysis

Overview

This project investigates the structural and physicochemical effects of major cancer-associated p53 mutations using BioPython and AlphaFold structural data.

Mutations Analyzed

• R175H
• G245S
• R248Q
• R273H
• R282W

Workflow

1. Retrieve p53 protein sequence from UniProt
2. Generate cancer-associated mutations
3. Calculate molecular properties
4. Download AlphaFold structure
5. Analyze structural confidence (pLDDT)
6. Map hotspot mutations
7. Predict mutation severity

Results

AlphaFold Confidence Profile

Hotspot Mutation Mapping

Mutation Severity Ranking

Key Findings

• All hotspot mutations occur within the DNA-binding domain.
• AlphaFold confidence scores exceeded 94 for all hotspot residues.
• R248Q exhibited the highest predicted impact.
• R282W showed substantial structural disruption potential.