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.
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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.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
Studies of conformational chan ...... rse-grained UNRES force field.
@en
type
label
Studies of conformational chan ...... rse-grained UNRES force field.
@en
prefLabel
Studies of conformational chan ...... rse-grained UNRES force field.
@en
P2093
P2860
P1476
Studies of conformational chan ...... rse-grained UNRES force field.
@en
P2093
Adam K Sieradzan
Agnieszka G Lipska
Magdalena A Mozolewska
Sabato D'Auria
P2860
P2888
P356
10.1007/S00894-015-2609-1
P577
2015-03-03T00:00:00Z