An investigation into the stability of α-crystallin by NMR spectroscopy; evidence for a two-domain structure

摘要: Abstract The stability of bovine lens α-crystallin with respect to temperature, pH and urea has been investigated by 1H 31P-NMR spectroscopy. spectra show little change temperature up 75°C, indicating that great thermal does not undergo any major in structure temperature. spectral studies its isolated αA αB subunits reveal a marked difference the these species. It is found that, at 2.5, αA-crystallin adopts native conformation whereas αB-crystallin denatured. On other hand, two when part total aggregate adopt but presence 0.1 M glycine become Thus, are more stable species than and, α-crystallin, there an interaction between compact domains leads enhanced stability. Finally, changes varying concentrations consistent two-domain model for C-terminal domain being less unfolding first urea.