Temperature dependent γH2AX binding to DNA

BINDING OF THE ANTITUMOR DRUG ADRIAMYCIN TO DNA-HISTONE COMPLEXES

Isotherms of the binding of the anthracycIine antibiotic, adriamycin (adriblastin), to DNA histone complexes was studied by means of spectroscopic analysis. The results indicated that: (a) binding of adriamycin to histones reduced the interaction of histones with DNA, (b) binding of the drug to DNA did not change the binding affinity of histone to DNA and, (c) in the explored binding range...

A temperature-dependent effective potential explains CO binding to myoglobin

Up to the onset of ligand escape from the heme pocket, CO binding to myoglobin can be explained by stochastic motion of the protein subject to an effective, temperature-dependent potential. Two "temperature-models" for the effective potential are investigated. The quantitative solution of the transient Smoluchowski equation for these models shows inhomogeneous kinetics at short times and protei...

Temperature dependent electron binding in (H2O)8.

We combine classical molecular dynamics simulations and quantum density functional theory calculations to study the temperature effects on the electron affinity of the water octamer. The atomistic simulations provide a sample of the cluster's conformations as a function of the temperature, on which the density functional calculations are carried on. As the temperature increases, the cluster und...

A microsome-dependent binding of benzo[a]pyrene to DNA.

The γH2AX DNA damage assay from a drop of blood

DNA double-strand breaks (DSB) and blocked replication forks activate the DNA damage response (DDR), a signaling pathway marked by phosphorylation of histone 2AX (H2AX). The phosphorylated form, γH2AX, accumulates at the site of damage and can be detected as foci by immunocytochemistry. Therefore, γH2AX is a sensitive and robust biomarker of DNA damage, notably DSB. Cells from peripheral blood ...