The result of molecular dynamics simulation. by Ashraf Attia Mahmoud (21262201)

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Extraction of demaging missense mutations from the TCGA Database. by Ashraf Attia Mahmoud (21262201)

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Structural alterations in hydrogen bond networks of the TP53 protein caused by mutations G266E (A-B), G105C (C-D), R273C (E-F), R280G (G-H), and Q136P (I-J). by Ashraf Attia Mahmoud (21262201)

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(A) The distribution of mutations within the 3D structure of the TP53 protein. by Ashraf Attia Mahmoud (21262201)

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The result of the secondary structure prediction of native and six mutant proteins of TP35 protein using the SOPMA server. by Ashraf Attia Mahmoud (21262201)

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Graph illustrating the distribution of mutations across 20 genes. by Ashraf Attia Mahmoud (21262201)

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Molecular dynamics simulation results for Apo-TP53 (red), wild-typeTP53. by Ashraf Attia Mahmoud (21262201)

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Effect of mutations on protein stability predicted by I-MUTANT 2.0, MUpro and CUPSAT. by Ashraf Attia Mahmoud (21262201)

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P53 mutant docking results (HDOCK and pyDOCK servers). by Ashraf Attia Mahmoud (21262201)

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Oncogenic Classification of TP53 missense mutations. by Ashraf Attia Mahmoud (21262201)

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Computational analysis of missense mutations using PhD-SNP, PANTHER and, SNPs&GO. by Ashraf Attia Mahmoud (21262201)

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Redocking results showing the interaction between the TP53 protein (white ribbon) and its DNA dodecamer ligand (magenta and blue) from PDB ID: 2AC0, highlighting the binding confor... by Ashraf Attia Mahmoud (21262201)

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Result of the phenotypic analysis. by Ashraf Attia Mahmoud (21262201)

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Oncogenic nature of mutations predicted using CScape and CScape-somatic. by Ashraf Attia Mahmoud (21262201)

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(A) Pie chart showing the distribution of mutation types identified within the TP53 gene. by Ashraf Attia Mahmoud (21262201)

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Structural clashes in TP53 mutants: (A) G266E mutation causes steric clashes with PHE109 and LEU257, destabilizing the structure. by Ashraf Attia Mahmoud (21262201)

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(A) TP53 expression levels are elevated in TP53-mutant and nonmutant HNSC samples compared to normal tissues. by Ashraf Attia Mahmoud (21262201)

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Type of Mutations. by Ashraf Attia Mahmoud (21262201)

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Probing the Histamine H₁ Receptor Binding Site to Explore Ligand Binding Kinetics by Sebastiaan Kuhne (1474948)

“…Ligand efficiency (LE) decreases upon the introduction of the negatively charged group, whereas kinetic efficiency (KE) increases up to 8.5-fold. …”

Probing the Histamine H₁ Receptor Binding Site to Explore Ligand Binding Kinetics by Sebastiaan Kuhne (1474948)

“…Ligand efficiency (LE) decreases upon the introduction of the negatively charged group, whereas kinetic efficiency (KE) increases up to 8.5-fold. …”