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Q51673743-4CD1D9F3-57BF-46C6-802B-3C4AF5FBE4F9
Q51673743-4CD1D9F3-57BF-46C6-802B-3C4AF5FBE4F9
BestRank
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http://www.wikidata.org/entity/statement/Q51673743-4CD1D9F3-57BF-46C6-802B-3C4AF5FBE4F9
Sequence- and Temperature-Dependent Properties of Unfolded and Disordered Proteins from Atomistic Simulations.
P2860
Q51673743-4CD1D9F3-57BF-46C6-802B-3C4AF5FBE4F9
BestRank
Statement
http://www.wikidata.org/entity/statement/Q51673743-4CD1D9F3-57BF-46C6-802B-3C4AF5FBE4F9
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wasDerivedFrom
8ab22c840461977064b01d93a4ee7615059b8647
P2860
Microsecond hydrophobic collapse in the folding of Escherichia coli dihydrofolate reductase, an alpha/beta-type protein.