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Q41321762-7583F1C6-C6F0-4A9F-9993-F5975D0898F6
Q41321762-7583F1C6-C6F0-4A9F-9993-F5975D0898F6
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http://www.wikidata.org/entity/statement/Q41321762-7583F1C6-C6F0-4A9F-9993-F5975D0898F6
Studies of conformational changes of an arginine-binding protein from Thermotoga maritima in the presence and absence of ligand via molecular dynamics simulations with the coarse-grained UNRES force field.
P2860
Q41321762-7583F1C6-C6F0-4A9F-9993-F5975D0898F6
BestRank
Statement
http://www.wikidata.org/entity/statement/Q41321762-7583F1C6-C6F0-4A9F-9993-F5975D0898F6
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wasDerivedFrom
b099d447c39aa8613fb1bd33c6643a43365179ea
P2860
Extension of UNRES force field to treat polypeptide chains with D-amino-acid residues.