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. Study holds ProTherm entries: 10810, 10811 Extra Details: alpha-crystallin; heat shock protein; scanning calorimetry;,conformational stability; non-productive folding form

Submission Details

ID: e5VFfrDe

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:41 p.m.

Version: 1

Publication Details
Gesierich U;Pfeil W,FEBS Lett. (1996) The conformational stability of alpha-crystallin is rather low: calorimetric results. PMID:8814280
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