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Q36470871-285165F8-5F27-4963-A3E0-B78A53250758
Q36470871-285165F8-5F27-4963-A3E0-B78A53250758
BestRank
Statement
http://www.wikidata.org/entity/statement/Q36470871-285165F8-5F27-4963-A3E0-B78A53250758
Small-angle X-ray scattering and single-molecule FRET spectroscopy produce highly divergent views of the low-denaturant unfolded state.
P2860
Q36470871-285165F8-5F27-4963-A3E0-B78A53250758
BestRank
Statement
http://www.wikidata.org/entity/statement/Q36470871-285165F8-5F27-4963-A3E0-B78A53250758
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wasDerivedFrom
786eacb87235df51387d1a28c325658ed334c230
P2860
Protein folding kinetics exhibit an Arrhenius temperature dependence when corrected for the temperature dependence of protein stability.