Journal article
Sugar-Induced Molten-Globule Model
Biochemistry (Easton), v 37(48), pp 17048-17053
01 Dec 1998
PMID: 9836600
Featured in Collection : UN Sustainable Development Goals @ Drexel
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.
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Details
- Title
- Sugar-Induced Molten-Globule Model
- Creators
- Paula R. Davis-Searles - University of North Carolina at Chapel HillArtemiza S. Morar - University of North Carolina at Chapel HillAleister J. Saunders - University of North Carolina at Chapel HillDorothy A. Erie - University of North Carolina at Chapel HillGary J. Pielak - University of North Carolina at Chapel Hill
- Publication Details
- Biochemistry (Easton), v 37(48), pp 17048-17053
- Publisher
- American Chemical Society; Washington, DC
- Number of pages
- 6
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biology
- Web of Science ID
- WOS:000077339600025
- Scopus ID
- 2-s2.0-0032374095
- Other Identifier
- 991021448155104721
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- Web of Science research areas
- Biochemistry & Molecular Biology