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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Gesierich U,Pfeil W

doi

10.1016/0014-5793(96)00867-8

subject

Has Abstract

pub_date

1996-09-16 00:00:00

pages

151-4

issue

2-3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(96)00867-8

journal_volume

393

pub_type

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