HIGHLIGHTS
SUMMARY
Molecular dynamics (MD) simulations have recently attempted to fill this gap, including development of new force_fields to accurately model disordered proteins (Best et_al, 2014; Rauscher et_al, 2015). Mutual consistency and complementarity have been demonstrated for the three most commonly used structural techniques for IDPs: Small Angle X-Ray Scattering (SAXS), Nuclear Magnetic Resonance (NMR) and single-molecule Förster Resonance Energy Transfer (smFRET) (Delaforge et_al, 2015; Aznauryan et_al, 2016; Voithenberg et_al, 2016; Fuertes et_al, 2017; Gomes et_al, 2020; Lincoff et_al, 2020; NaudiFabra et_al, 2021). Improvements in the accuracy of MD force_fields, which correct earlier . . .
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