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Q30159730-217253F1-86F3-4EB8-8A1D-2D91DE1A502E
Q30159730-217253F1-86F3-4EB8-8A1D-2D91DE1A502E
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http://www.wikidata.org/entity/statement/Q30159730-217253F1-86F3-4EB8-8A1D-2D91DE1A502E
Similarity and difference in the unfolding of thermophilic and mesophilic cold shock proteins studied by molecular dynamics simulations
P2860
Q30159730-217253F1-86F3-4EB8-8A1D-2D91DE1A502E
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http://www.wikidata.org/entity/statement/Q30159730-217253F1-86F3-4EB8-8A1D-2D91DE1A502E
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ab3e4d1f47333393f04a8fa94e249303af65b50b
P2860
Experiment and theory highlight role of native state topology in SH3 folding.