Journal
BIOPHYSICAL JOURNAL
Volume 97, Issue 10, Pages 2803-2810Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2009.08.046
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Funding
- National Science Foundation
- National Institutes of Health [RO1 GM068460]
- Division of Biology and Biomedical Science of Washington University in St. Louis
- Computational Biology Training [GM 008802]
- Kauffman Foundation
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Mini-proteins that contain <50 amino acids often serve as model systems for studying protein folding because their small size makes long timescale simulations possible. However, not all mini-proteins are created equal. The stability and structure of FSD-1, a 28-residue mini-protein that adopted the beta beta alpha zinc-finger motif independent of zinc binding, was investigated using circular dichroism, differential scanning calorimetry, and replica-exchange molecular dynamics. The broad melting transition of FSD-1, similar to that of a helix-to-coil transition, was observed by using circular dichroism, differential scanning calorimetry, and replica-exchange molecular dynamics. The N-terminal beta-hairpin was found to be flexible. The FSD-1 apparent melting temperature of 41 degrees C may be a reflection of the melting of its alpha-helical segment instead of the entire protein. Thus, despite its attractiveness due to small size and purposefully designed helix, sheet, and turn structures, the status of FSD-1 as a model system for studying protein folding should be reconsidered.
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