Exploring interfacial dynamics in homodimeric S-ribosylhomocysteine lyase (LuxS) from Vibrio cholerae through molecular dynamics simulations
Keyword(s):
To the best of our knowledge, this is the first molecular dynamics simulation study on the dimeric form of the LuxS enzyme from Vibrio cholerae to evaluate its structural and dynamical properties including the dynamics of the interface formed by the two monomeric chains of the enzyme.
2020 ◽
Vol 22
(3)
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pp. 1154-1167
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2015 ◽
Vol 17
(45)
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pp. 30307-30317
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2015 ◽
Vol 17
(41)
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pp. 27840-27850
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2020 ◽
Vol 22
(20)
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pp. 11400-11408
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