Conformational dynamics and structural plasticity play critical roles in the ubiquitin recognition of a UIM domain.

Folding cooperativity and dynamics of a Ubiquitin/UIM fusion protein by NMR, DSC, CD, fluorescence experiments and MD simulations

Solution Structure Of A UbiquitinUIM FUSION PROTEIN

ubiquitin-60S ribosomal protein L40 [Kluyveromyces marxianus DMKU3-1042]

unnamed protein product [Kluyveromyces dobzhanskii CBS 2104]

ubiquitin-40S ribosomal protein S27b, partial [Candida albicans P37005]

polyubiquitin, partial [Candida albicans P78048]

ubiquitin-60S ribosomal protein L40, partial [Candida albicans 12C]

ubiquitin-60S ribosomal protein L40, partial [Candida albicans P75063]

polyubiquitin, partial [Candida albicans P37039]

engineered protein fusion construct: modified yeast Ubiquitin c-terminally linked to the UIM helix of Vps27

Solution structure of a Ubiquitin/UIM fusion protein

simulated annealing, torsion angle dynamics, molecular dynamics, energy minimization

acrylamide/N,N'-methylenebisacrylamide gel 83:1