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Q51636215-927DCF47-A0E5-44F9-9529-8E126835FF16
Q51636215-927DCF47-A0E5-44F9-9529-8E126835FF16
BestRank
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http://www.wikidata.org/entity/statement/Q51636215-927DCF47-A0E5-44F9-9529-8E126835FF16
Picosecond to nanosecond dynamics provide a source of conformational entropy for protein folding.
P2860
Q51636215-927DCF47-A0E5-44F9-9529-8E126835FF16
BestRank
Statement
http://www.wikidata.org/entity/statement/Q51636215-927DCF47-A0E5-44F9-9529-8E126835FF16
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wasDerivedFrom
e454c87dc3b8e39161fdce003065da887bc4316d
P2860
Dynamical coupling of intrinsically disordered proteins and their hydration water: comparison with folded soluble and membrane proteins