A methodological study has been undertaken to assess the conformational profile of Neuromedin B
(NMB) using classical molecular dynamics simulations (MD) and replica exchange molecular dynamics
(REMD) simulations under generalized Born (GB) solvent conditions. Comparison of the results obtained
from these simulations suggests that the peptide has a propensity to adopt both b-turns and a-helical
conformations regardless of the simulation protocols used. However, the conformations adopted more
hel...
A methodological study has been undertaken to assess the conformational profile of Neuromedin B
(NMB) using classical molecular dynamics simulations (MD) and replica exchange molecular dynamics
(REMD) simulations under generalized Born (GB) solvent conditions. Comparison of the results obtained
from these simulations suggests that the peptide has a propensity to adopt both b-turns and a-helical
conformations regardless of the simulation protocols used. However, the conformations adopted more
helical character under REMD conditions and showed good agreement with the NMR supported structure
reported in the literature.
Citació
Sharma, P. [et al.]. A computational study of Neuromedin B. "Computational and theoretical chemistry", 15 Setembre 2011, vol. 971, núm. 1-3, p. 1-7.
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