255 research outputs found

    Most Admired Leader/Most Admired Follower

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    In introducing concepts of leadership and followership to students, this experiential exercise highlights qualities associated with the leader and follower roles. Various learning objectives guide the development of the exercise. They focus on identification of behavioral qualities possessed by both leaders and followers and on the importance of the leader-follower relationship to the organization’s achievement of goals. Theoretical underpinnings are stressed throughout. In the exercise, students individually develop a list of characteristics associated with their own most admired leader or follower and then share their lists in small groups. In plenary discussion, groups share all characteristics identified, and the instructor leads discussion to achieve stated learning objectives. Exercise handouts, instructions for facilitating classroom discussion, and a summary of theories that may be used as a postexercise student handout are provided

    Changes in Dynamics upon Oligomerization Regulate Substrate Binding and Allostery in Amino Acid Kinase Family Members

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    Oligomerization is a functional requirement for many proteins. The interfacial interactions and the overall packing geometry of the individual monomers are viewed as important determinants of the thermodynamic stability and allosteric regulation of oligomers. The present study focuses on the role of the interfacial interactions and overall contact topology in the dynamic features acquired in the oligomeric state. To this aim, the collective dynamics of enzymes belonging to the amino acid kinase family both in dimeric and hexameric forms are examined by means of an elastic network model, and the softest collective motions (i.e., lowest frequency or global modes of motions) favored by the overall architecture are analyzed. Notably, the lowest-frequency modes accessible to the individual subunits in the absence of multimerization are conserved to a large extent in the oligomer, suggesting that the oligomer takes advantage of the intrinsic dynamics of the individual monomers. At the same time, oligomerization stiffens the interfacial regions of the monomers and confers new cooperative modes that exploit the rigid-body translational and rotational degrees of freedom of the intact monomers. The present study sheds light on the mechanism of cooperative inhibition of hexameric N-acetyl-L-glutamate kinase by arginine and on the allosteric regulation of UMP kinases. It also highlights the significance of the particular quaternary design in selectively determining the oligomer dynamics congruent with required ligand-binding and allosteric activities
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