Abstract：
:Proteins denature at low pH because of intramolecular electrostatic repulsions. The addition of salt partially overcomes this repulsion for some proteins, yielding a collapsed conformation called the A-state. A-states have characteristics expected for the molten globule, a notional kinetic protein folding intermediate. Here we show that the addition of neutral sugars to solutions of acid-denatured equine ferricytochrome c induces formation of the A-state in the absence of added salt. We characterized the structure and stability of the sugar-induced A-state with circular dichroism spectropolarimetry (CD) and NMR-monitored hydrogen-deuterium exchange experiments. We also examined the stability of the sugar-induced A-state as a function of sugar size and concentration. The results are interpreted using several models and we conclude that the stabilizing effect is consistent with increased steric repulsion between the protein and the sugar solutions.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Davis-Searles PR,Morar AS,Saunders AJ,Erie DA,Pielak GJdoi
10.1021/bi981364vsubject
Has Abstractpub_date
1998-12-01 00:00:00pages
17048-53issue
48eissn
0006-2960issn
1520-4995pii
bi981364vjournal_volume
37pub_type
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