Conformational Change in Unsolvated Trp-cage Protein Probed by Fluorescence
- 27 May 2005
- journal article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 127 (24), 8606-8607
- https://doi.org/10.1021/ja051788u
Abstract
We report the first direct measurements of the unfolding of a protein, Trp-cage, in the gas phase using laser-induced fluorescence of protein ions in a heated quadrupole ion trap. The changes in enthalpy and entropy associated with the observed conformational change are obtained by fitting a two-state model of protein unfolding to the fluorescence intensities plotted versus temperature. The enthalpy and entropy changes for the 2+ and 3+ charge states are greater than the values measured in solution and depend on charge state.Keywords
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