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Q30564434-6BE67D4B-12E8-4709-B93A-65212ECF7EE5
Q30564434-6BE67D4B-12E8-4709-B93A-65212ECF7EE5
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http://www.wikidata.org/entity/statement/Q30564434-6BE67D4B-12E8-4709-B93A-65212ECF7EE5
A comparison of the folding kinetics of a small, artificially selected DNA aptamer with those of equivalently simple naturally occurring proteins.
P2860
Q30564434-6BE67D4B-12E8-4709-B93A-65212ECF7EE5
BestRank
Statement
http://www.wikidata.org/entity/statement/Q30564434-6BE67D4B-12E8-4709-B93A-65212ECF7EE5
rank
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type
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wasDerivedFrom
706098d3840c2c44a8f4e4cf9fc39ead3800135c
P2860
Small-angle X-ray scattering and single-molecule FRET spectroscopy produce highly divergent views of the low-denaturant unfolded state.