The thermal stability of native, delipidated, deionized and regenerated bacteriorhodopsin

✍ Scribed by G.C. Kresheck; C.T. Lin; L.N. Williamson; W.R. Mason; D.-J. Jang; M.A. El-Sayed

• Book ID: 103993134
• Publisher: Elsevier Science
• Year: 1990
• Tongue: English
• Weight: 679 KB
• Volume: 7
• Category: Article
• ISSN: 1011-1344
• DOI: 10.1016/1011-1344(90)85163-q

✦ Synopsis

Differential scanning calorimetry curves and circular dichroism spectra were determined for native bacteriorhodopsin (bR), deionized bR, acid blue and acid purple bR, 75% delipidated bR, deionized-delipidated bR and Mg ~ + regenerated deionized bR. The effects of the different perturbations on the thermal stability (melting temperature) and the apparent helical content of the protein were examined. These perturbations have more influence on the deprotonation efficiency and the color change of retinal than on the thermal stability and the apparent helical content of the protein. Although the addition of Mg 2+ to deionized bR restores the photochemical cycle, it does not restore the thermal stability to that of the native material.