title: The conformational stability of alpha-crystallin is rather low: calorimetric results.
abstract: The eye lens protein and chaperonin, alpha-crystallin, was studied by differential scanning microcalorimetry, spectroscopy and size exclusion chromatography. The thermal transition of alpha-crystallin proceeds at Ttrs = 59.8 +/- 0.6 degrees C with an enthalpy change of delta H = 336 +/- 9 kJ per mol subunit. Disagreement between previous delta H values could be attributed to a side reaction that leads, depending on the scan rate, to the formation of a non-productive folding form. The conformational stability of alpha-crystallin is rather low (delta G = 24 +/- 5 kJ/mol of subunit). The minimal cooperative unit of alpha-crystallin is the monomeric subunit.
authors.affiliation: University of Potsdom, Max-Delbrück-Centre for Molecular Medicine, Berlin-Buch, Germany.
authors.forename: U
authors.initials: U
authors.lastname: Gesierich
authors.forename: W
authors.initials: W
authors.lastname: Pfeil
mesh_terms: D000818:Animals; D002152:Calorimetry, Differential Scanning; D002417:Cattle; D003459:Crystallins / Q000737:chemistry*; D004355:Drug Stability; D007908:Lens, Crystalline; D011487:Protein Conformation; D011489:Protein Denaturation; D013816:Thermodynamics
chemical_list: D003459:Crystallins