Stability of p53 homologs.

Here we investigate the thermal stability, secondary structure and folding properties of the DNA-binding domains (DBDs) of a range of proteins from the p53 family using

NRs are characterized by significant amino acid sequence similarities in two key functional domains: the DNA binding domain (DBD), which directs the sequence-specific DNA-binding of

The conserved Myb DNA binding domain and the interacting domains for Snapc1/snapc5 and Snapc2 as described for the human SNAPC4 ([16,17] are indicated by boxes. The m1045

To quantify the effect of SOX2 on the DNA-binding affinity of OCT4, we calculated the un- binding free energy profile for each of its domains from the biased simulations.. Then,

Figure S8 Structure-based sequence alignment of the crystallized VosA fragment with NF k B (PDB ID code 1SVC) and VelB reveals a high structural similarity in the canonical fold

was performed to corroborate the experimental results, by predicting the binding mode, relative binding energy of the complex formed between β -carboline derivatives with DNA and

49 The quenching and binding constants of ruthenium(II) complexes indicate that the interaction of tested compounds with CT-DNA should be of intercalation.. DNA-binding study

Here we use a combination of in vitro and in vivo studies to show that maize CENPC has both DNA-binding and RNA-binding capacities, that the DNA/RNA-binding domain is localized to