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• W2029349765 endingPage "14244" @default.
• W2029349765 startingPage "14241" @default.
• W2029349765 abstract "By using titin as a model system, we have demonstrated that fluorescence quenching can be used to study protein folding at the single molecule level. The unfolded titin molecules with multiple dye molecules attached are able to fold to the native state. In the native folded state, the fluorescence from dye molecules is quenched due to the close proximity between the dye molecules. Unfolding of the titin leads to a dramatic increase in the fluorescence intensity. Such a change makes the folded and unfolded states of a single titin molecule clearly distinguishable and allows us to measure the folding dynamics of individual titin molecules in real time. We have also shown that fluorescence quenching can signal folding and unfolding of a small protein with only one immunoglobulin domain." @default.
• W2029349765 created "2016-06-24" @default.
• W2029349765 creator A5001967033 @default.
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• W2029349765 date "2000-12-19" @default.
• W2029349765 modified "2023-10-14" @default.
• W2029349765 title "Fluorescence quenching: A tool for single-molecule protein-folding study" @default.
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• W2029349765 doi "https://doi.org/10.1073/pnas.97.26.14241" @default.
• W2029349765 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/18902" @default.
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