According to the focal article by Britt, Shen, Sinclair, Grossman, and Klieger (2016), it seems conclusive that all definitions of resilience involve an experience of significant adversity, regardless of whether it is examined as a trait or an outcome. This experience of adversity is inherently emotional. When considering the ability or outcome of “bouncing back” from a stressful or chronic event, one must recognize the emotional experience and consider how individuals may cope with their emotions. This said, there is a clear connection between resilience and emotion regulation. The focal article presents a descriptive model of resilience for employees, which includes mention of energy and affect as individual resources but does not acknowledge the connection between resilience and emotion regulation. In this commentary I argue that these two research areas are related but largely neglected in the current literature. I will discuss the (a) process model of emotion regulation, (b) points of connection with resilience, and (c) empirical research suggesting the importance of positive emotion.

The pyridoxal phosphate (PLP) dependent enzyme dialkylglycine decarboxylase (DGD) specifically binds alkali metal ions near the active site. Large ions (Rb + , K + ) activate the enzyme while smaller ones (Na + , Li + ) inhibit it. Crystallographic results have shown that DGD undergoes a metal ion size dependent structural switch [Hohenester, E., Keller, J. W., and Jansonius, J. N. (1994) Biochemistry 33, 13561], but no evidence for multiple conformations in crystalline DGD was obtained. Here, evidence is presented that DGD-K + in solution exists in two conformations differing in catalytic competence. Initial rate traces for DGD-K + exhibit a high degree of curvature due to decreasing activity over time. DGD remains tetrameric under the assay conditions as demonstrated by gel filtration experiments, arguing against the possibility of subunit dissociation as the source of activity loss. Likewise, the mass spectrum of DGD shows a single covalent form. A hysteretic model that assumes two slowly interconverting enzyme forms accounts well for the initial rate data when kinetic parameters from biphasic pre-steady-state kinetics are employed. The fit of the model to the data yields an estimate of 59 ( 1% for the fast form. A cooperative model cannot account for the data. Double reciprocal plots for coenzyme binding to DGD exhibit two linear phases. Similarly, two kinetic phases are observed in PLP association kinetics. The substitution of Na + or Rb + for K + alters the steady-state kinetic parameters of DGD. Preincubation of DGD-K + with the competitive inhibitor 1-aminocyclopropane-1-carboxylate (ACC) lowers both k cat and K AIB apparently by drawing the enzyme toward the less active, tighter binding form observed in the presteady-state kinetics. These results suggest that the structure of the protein around the alkali metal ion determines the conformational distribution. The transamination reaction with L-alanine was coupled in the pre-steady-state to the LDH-catalyzed oxidation of NADH. This experiment yields an estimate of 68 ( 4% for the fast form, in agreement with the hysteretic fit to the steady-state data. The reaction of DGD with dithiobis(nitrobenzoate) was used to probe the preexisting forms of DGD. Preincubation of DGD with ACC, like the exchange of Na + for K + , shifts the conformational distribution, in agreement with the steady-state kinetics. These experiments clearly demonstrate that DGD is a hysteretic enzyme whose conformational distribution is controlled by the identity of the alkali metal ion bound near the active site, and that cooperativity does not play a role in catalysis or regulation.2,2-Dialkylglycines occur naturally as major constituents of fungal peptide antibiotics (1, 2). The catabolic processing of these amino acids in soil bacteria (3) and fungi (4) occurs through the pyridoxal 5′-phosphate (PLP) 1 dependent 2,2-dialkylglycine decarboxylase. DGD catalyzes the oxidative decarboxylation of 2,2-dialkylglycines in the first halfreaction of its ping-pong kinetic mechanism, fo...

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The ideologically objectionable premise model posits that biased political judgments can emerge across the political spectrum. Previous tests of ideological differences in political judgment biases have utilized between-subjects designs (i.e., separate comparisons). In this study ( N = 410), we examined whether these biases also emerge in within-subjects designs (i.e., joint comparisons) and compared the strengths of judgment biases in between-subjects and within-subjects designs. Across designs, both liberals and conservatives favored sympathetic over unsympathetic targets in scenario judgments, but biases were attenuated in the within-subjects design. No ideological differences in bias strength emerged, although liberals reported a stronger internal motivation to respond without prejudice toward ideologically dissimilar others. Further, consistent with the ideological conflict hypothesis, both liberals and conservatives were prejudiced toward ideologically dissimilar targets, although biases in prejudice ratings were stronger among liberals than conservatives. Together, results support the ideological symmetry perspective on political bias and prejudice.

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