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Q27670631-5EF68DF6-CE14-4711-9541-0EE0B6CCD652
Q27670631-5EF68DF6-CE14-4711-9541-0EE0B6CCD652
BestRank
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http://www.wikidata.org/entity/statement/Q27670631-5EF68DF6-CE14-4711-9541-0EE0B6CCD652
Stabilizing Salt-Bridge Enhances Protein Thermostability by Reducing the Heat Capacity Change of Unfolding
P2860
Q27670631-5EF68DF6-CE14-4711-9541-0EE0B6CCD652
BestRank
Statement
http://www.wikidata.org/entity/statement/Q27670631-5EF68DF6-CE14-4711-9541-0EE0B6CCD652
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wasDerivedFrom
5ffdaf33966a823005ad3af2af7807fd9594fc83
P2860
Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water.