3o81

Publication Abstract from PubMed

beta(2)-microglobulin (beta(2)m) is the smallest building block of molecules belonging to the immunoglobulin superfamily. By comparing thermodynamic and structural characteristics of chicken beta(2)m with those of other species, we seek to elucidate whether it is possible to pinpoint features that set the avian protein apart from other beta(2)m. The thermodynamic assays revealed that chicken beta(2)m exhibits a lower melting temperature than human beta(2)m, and the H/D exchange behavior observed by infrared spectroscopy indicates a more flexible structure of the former protein. To understand these differences at a molecular level, we determined the structure of free chicken beta(2)m by X-ray crystallography to a resolution of 2.0 A. Our comparisons indicate that certain biophysical characteristics of the chicken protein, particularly its conformational flexibility, diverge considerably from those of the other beta(2)m analyzed, although basic structural features have been retained through evolution.

Comparative biophysical characterization of chicken beta2-microglobulin.,Hee CS, Fabian H, Uchanska-Ziegler B, Ziegler A, Loll B Biophys Chem. 2012 Jun;167:26-35. doi: 10.1016/j.bpc.2012.04.001. PMID:22695053^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.