BH3 proteins from the professional apoptotic family members have been used to understand and study Bcl 2 family function and specificity. three changes are more likely to be significant, because these remains are part of the uncovered hydrophobic groove in Bcl xL and were found to contact the Bak peptide in the structure of the Bak peptide/Bcl xL complicated. We used a polarization assay to assess the affinity of BHRF1 for BH3 peptides in the proteins Bak, ALK inhibitor Bax, Bad, Bik and Bid, to investigate the binding desire for BHRF1. Surprisingly, BHRF1 confirmed no binding to Bak, Bad, Bik o-r Bax in this analysis. Earlier studies indicated that BHRF1 didn’t bind to full length Bax;however, binding to full length Bak was observed. The only real considerable binding that people could recognize for BHRF1 was to the BH3 peptide from Bid. This binding was weak,,800 nM, and much less compared to the binding of the other anti apoptotic proteins to BH3 peptides. Early in the day reports suggested a connection between BHRF1 and the anti apoptotic family unit members Bcl xL and Bcl 2. To use and verify these results we tested for binding using pure proteins in an in vitro assay that used heteronuclear single quantum coherence spectra to check for spectral changes that would occur upon binding. Under our conditions, we noticed no spectral change indicative of binding. Since the Lymphatic system BH3 region of BHRF1 is hidden and not exposed in the framework, we tried to see if we can discover binding between Bcl xL and a peptide in the BHRF1 BH3 region. The BHRF1 BH3 peptide DTVVLRYHVLLEEIIER didn’t bind to Bcl xL. These data do not support early in the day studies, in which binding to Bcl xL was reported,or future studies using full-length GST BHRF1 in a pull down assay that suggested binding to Bcl 2 but not to Bcl xL. A substantial difference between our studies and the earlier work is the fact that we have used soluble constructs of of the proteins in our binding studies. The next Bcl 2 homolog of EBV, BALF1, is reported to behave as a regulator of BHRF1. We tried to see if a peptide from the BH3 domain of BALF1 bound to BHRF1. Again, we did not find any binding, employing a 15N HSQC array to check for spectral changes. This is in keeping with early in the day studies, which indicated that both proteins do not co localize inside cells. The 3d answer composition of the EBV Bcl 2 homolog BHRF1 is quite much like those of other Deubiquitinase inhibitors Bcl 2 members of the family. However, unlike other anti apoptotic Bcl 2 family members,BHRF1 does not have a distinct hydrophobic groove. This absence of a binding groove might explain the results of our binding reports, which showed that BHRF1 didn’t bind to the peptide mimics of the BH3 domains of Bak, Bad, Bik o-r Bax.