Characterization of interfaces

Bovine seminal ribonuclease (BS-RNase) is the only known dimeric enzyme characterized by an equilibrium between two different 3D structures: MxM, with exchange (or swapping) of the N-terminal 1–20 residues, and M¼M, without exchange. As a consequence, the hinge region 16–22 has a different tertiary structure in the two forms. In the native protein, the equilibrium ratio between MxM and M¼M is about 7 : 3.

7p fptmusic 12-04-2013 42 3   Download

Hepatocyte nuclear factor-4 (HNF-4a), a member of the nuclear receptor superfamily, binds DNA exclusively as a homodimer. Dimerization con-trols important aspects of receptor function, such as DNA binding, protein stability, ligand binding and interaction with coactivators.

11p inspiron33 26-03-2013 45 5   Download

This study of the full-length bifunctional nonstructural protein 3 from hep-atitis C virus (HCV) has revealed that residues in the helicase domain affect the inhibition of the protease. Two residues (Q526 and H528), appar-ently located in the interface between the S2 and S4 binding pockets of the substrate binding site of the protease, were selected for modification, and three enzyme variants (Q526A, H528A and H528S) were expressed, puri-fied and characterized.

8p media19 05-03-2013 34 4   Download

Enzymes from psychrophiles show higher catalytic efficiency in the 0–20C temperature range and often lower thermostability in comparison with meso⁄thermophilic homologs. Physical and chemical characterization of these enzymes is currently underway in order to understand the molecular basis of cold adaptation.

14p media19 04-03-2013 24 1   Download

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành hóa học dành cho các bạn yêu hóa học tham khảo đề tài: Nanoscale characterization of electrical transport at metal/3C-SiC interfaces

5p sting05 09-02-2012 52 3   Download