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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Gesierich U,Pfeil Wdoi
10.1016/0014-5793(96)00867-8subject
Has Abstractpub_date
1996-09-16 00:00:00pages
151-4issue
2-3eissn
0014-5793issn
1873-3468pii
0014-5793(96)00867-8journal_volume
393pub_type
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