Structural and functional investigation of the DHH/DHHA1 family proteins in Deinococcus radiodurans.

DHH/DHHA1 family proteins have been proposed to play critical roles in bacterial resistance to environmental stresses. Members of the most radioresistant bacteria genus, Deinococcus, possess two DHH/DHHA1 family proteins, RecJ and RecJ-like. While the functions of Deinococcus radiodurans RecJ (DrRecJ) in DNA damage resistance have been well characterized, the role and biochemical activities of D.

Structural and DNA end resection study of the bacterial NurA-HerA complex.

Background: The nuclease NurA and the ATPase/translocase HerA play a vital role in repair of double-strand breaks (DSB) during the homologous recombination in archaea. A NurA-HerA complex is known to mediate DSB DNA end resection, leading to formation of a free 3' end used to search for the homologous sequence. Despite the structures of individual archaeal types of NurA and HerA having been reported, there is limited information regarding the molecular mechanisms underlying this process.

Modified Tong Xie Yao Fang relieves solitary rectal ulcer syndrome: A case report.

Background: Solitary rectal ulcer syndrome (SRUS) is a rare rectal disorder characterized by bloody mucus in the stool, difficulty in defecation, pain, and anal swelling. To date, the etiology of this syndrome remains not well understood and the diagnosis is frequently confused with other disorders, making treatment a clinical challenge.

Case Summary: A 50-year-old woman presented to our hospital with a 40-d history of bloody mucus in the stool and anal swelling.

Identification differential behavior of Gd@C(OH) upon interaction with serum albumin using spectroscopic analysis.

The interaction between Gd@C(OH) and serum albumin (HSA and BSA) were investigated by spectroscopic analysis. From the characteristic feature of fluorescence quenching spectra at different temperatures, the inherent binding information including quenching mechanism, association constants, number of binding site, fraction of initial fluorescence and basic thermodynamic parameters were calculated. The binding of Gd@C(OH) to serum albumin caused strong quenching of protein intrinsic fluorescence and the structural changes of serum albumin.