Detecting molecular interactions that stabilize native bovine rhodopsin.

摘要: Using single-molecule force spectroscopy we probed molecular interactions within native bovine rhodopsin and discovered structural segments of well-defined mechanical stability. Highly conserved residues among G protein-coupled receptors were located at the interior individual segments, suggesting a dual role for these in rhodopsin. Firstly, stabilize secondary structure elements protein, secondly, they position hold highly functionally important environments. Two main classes curves observed. One class corresponded to unfolding with Cys110-Cys187 disulfide bond remaining intact other entire polypeptide chain. In absence bond, nature certain folded was altered. These changes highlight importance this may form basis dysfunctions associated its absence.