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Q30167659-16BFA658-2186-4A18-87E6-F728B107A0DA
Q30167659-16BFA658-2186-4A18-87E6-F728B107A0DA
BestRank
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http://www.wikidata.org/entity/statement/Q30167659-16BFA658-2186-4A18-87E6-F728B107A0DA
Protein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after the structural collapse
P2860
Q30167659-16BFA658-2186-4A18-87E6-F728B107A0DA
BestRank
Statement
http://www.wikidata.org/entity/statement/Q30167659-16BFA658-2186-4A18-87E6-F728B107A0DA
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wasDerivedFrom
254a589e772ba265e45de9ce0f57239051f54f3e
P2860
NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions.