Fig. 4
From: Slow conformational exchange and overall rocking motion in ubiquitin protein crystals
Intermolecular and intramolecular interactions that affect β-turn motion. a, b Intermolecular interactions involving the β-turn region in MPD-ub. Neighboring molecules are shown in light blue. Simulations of ubiquitin mutants suggest that these interactions are not responsible for causing the preference for βII, see text. c, d The surrounding of E24 side chain in different crystal forms of ubiquitin. c A rare frame from the MPD-ub trajectory where E24 side chain (painted red) is projected toward solvent. d A typical frame from cubic-PEG-ub trajectory where E24 from ubiquitin molecule chain A is immersed into solvent
