Acid-induced folding of proteins.
The addition of HCl, at low ionic strength, to the native state of apomyoglobin, beta-lactamase, and cytochrome c caused these proteins to adopt an essentially fully unfolded conformation in the vicinity of pH 2. However, contrary to expectation, the addition of further acid resulted in refolding to a compact conformation with the properties of a molten globule. The major factor responsible for the refolding is believed to be the binding of the anion, which minimizes the intramolecular charge repulsion that initially brought about the unfolding.
Goto
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Department of Chemistry, University of California, Santa Cruz 95064.
Calciano
L J
LJ
Fink
A L
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D000818:Animals; D001059:Apoproteins / Q000378:metabolism; D002942:Circular Dichroism; D003574:Cytochrome c Group / Q000378:metabolism; D006736:Horses; D006851:Hydrochloric Acid; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009211:Myoglobin / Q000378:metabolism; D010405:Penicillinase / Q000378:metabolism; D011487:Protein Conformation; D011489:Protein Denaturation; D011506:Proteins / Q000378:metabolism; D013056:Spectrophotometry, Ultraviolet
D001059:Apoproteins; D003574:Cytochrome c Group; D009211:Myoglobin; D011506:Proteins; C010857:apomyoglobin; D010405:Penicillinase; D006851:Hydrochloric Acid