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Q36590696-3C3B61F4-E89A-4DC7-9696-CA22057F4F8F
Q36590696-3C3B61F4-E89A-4DC7-9696-CA22057F4F8F
BestRank
Statement
http://www.wikidata.org/entity/statement/Q36590696-3C3B61F4-E89A-4DC7-9696-CA22057F4F8F
Protein folding kinetics exhibit an Arrhenius temperature dependence when corrected for the temperature dependence of protein stability.
P2860
Q36590696-3C3B61F4-E89A-4DC7-9696-CA22057F4F8F
BestRank
Statement
http://www.wikidata.org/entity/statement/Q36590696-3C3B61F4-E89A-4DC7-9696-CA22057F4F8F
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type
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Statement
wasDerivedFrom
56cef0e6b34196f2027188bdd36811ab40a9a00c
P2860
A desolvation barrier to hydrophobic cluster formation may contribute to the rate-limiting step in protein folding.