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Q30428863-5B866DAA-777B-4E1A-B1E9-CE6A80FCF01B
Q30428863-5B866DAA-777B-4E1A-B1E9-CE6A80FCF01B
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http://www.wikidata.org/entity/statement/Q30428863-5B866DAA-777B-4E1A-B1E9-CE6A80FCF01B
Molecular dynamics of individual alpha-helices of bacteriorhodopsin in dimyristol phosphatidylocholine. I. Structure and dynamics.
P2860
Q30428863-5B866DAA-777B-4E1A-B1E9-CE6A80FCF01B
BestRank
Statement
http://www.wikidata.org/entity/statement/Q30428863-5B866DAA-777B-4E1A-B1E9-CE6A80FCF01B
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wasDerivedFrom
3a56df6cc941f111a9fed38d807f924d591ab14f
P2860
Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis