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Objective The Four Square Step Test (FSST) is a tool that assesses dynamic balance during obstacle step-over. To date, few studies have used the FSST to measure balance in patients with Parkinson’s disease (PD). This study aimed to verify that patients with PD, even at the de novo early stage, take more time to perform the FSST and identify which factors, cognitive status or cardinal motor symptoms, are related most to FSST scores.Methods Thirty-five newly diagnosed drug-naïve patients with PD and 17 controls completed the FSST. The Unified Parkinson’s Disease Rating Scale (UPDRS), Hoehn and Yahr (H&Y) stage, spatiotemporal gait parameters, and neuropsychological test battery were also assessed in the PD group.Results Mean FSST performance time was 8.20 ± 1.61 seconds in patients with PD, which was significantly more than the control group (7.13 ± 1.10 seconds, p = 0.018). UPDRS part III total score and H&Y stage were not significantly associated with FSST, but among the UPDRS subscores, only the postural instability/gait disturbance subscore showed a significant association. Regarding the association between FSST and cognition, the Trail Making Test-B and the Color Word Stroop Test showed strongly inverse correlations with FSST (rho = -0.598 and -0.590, respectively). With respect to gait parameters, double support time was significantly associated with FSST score (rho = 0.342, p = 0.044); however, other parameters, including velocity and step length, were not associated with the FSST.Conclusion The FSST can be used in the clinic to assess dynamic balance with cognitive demands even in the early stages of PD.

Obtaining a quantitative description of the membrane proteins stability is crucial for understanding many biological processes. However the advance in this direction has remained a major challenge for both experimental studies and molecular modeling. One of the possible directions is the use of coarse-grained models but such models must be carefully calibrated and validated. Here we use a recent progress in benchmark studies on the energetics of amino acid residue and peptide membrane insertion and membrane protein stability in refining our previously developed coarse-grained model (Vicatos et al., Proteins 2014;82:1168). Our refined model parameters were fitted and/or tested to reproduce water/membrane partitioning energetics of amino acid side chains and a couple of model peptides. This new model provides a reasonable agreement with experiment for absolute folding free energies of several β-barrel membrane proteins as well as effects of point mutations on a relative stability for one of those proteins, OmpLA. The consideration and ranking of different rotameric states for a mutated residue was found to be essential to achieve satisfactory agreement with the reference data.