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Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES
Author(s) -
Peralta Dadna,
Hartman Dallas J.,
Hoogenraad Nicholas J.,
Høj Peter B.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80381-1
Subject(s) - chaperonin , groel , groes , chemistry , protein folding , folding (dsp implementation) , biochemistry , biophysics , biology , escherichia coli , electrical engineering , gene , engineering
Pig heart mitochondrial malate dehydrogenase was chemically denatured in guanidine HCl. Upon 50‐fold dilution of the denaturant spontaneous refolding could be observed in the temperature range 12–32°C. At 36°C spontaneous refolding was not observed but a stable folding intermediate that is fairly resistant to aggregation was formed. This intermediate is readily refolded by the chaperonins GroEL and GroES and may prove useful in future attempts to describe several aspects of chaperonin action at physiological temperatures.