489 research outputs found

    Improving The Oral Presentation Skills Of Accounting Students: An Experiment

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    Numerous surveys of accounting professionals have established the importance of communication skills for newly-hired accounting graduates, and challenge business schools to revise curricula accordingly. To determine if the oral skills of accounting students can be improved, two oral presentation assignments were given to students in six accounting classes at a small western university. The oral presentations were evaluated on ten oral communication skills recently judged by accounting professionals to be most important for new hires to possess. Feedback was provided after the first presentation. Results showed that oral presentation skills improved significantly after the first presentation. Accounting students can improve their oral presentation skills if the accounting faculty is committed to providing timely feedback

    Structures of the Neisseria meningitides methionineā€binding protein MetQ in substrate-free form and bound to L- and D-methionine isomers

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    The bacterial periplasmic methionineā€binding protein MetQ is involved in the import of methionine by the cognate MetNI methionine ABC transporter. The MetNIQ system is one of the few members of the ABC importer family that has been structurally characterized in multiple conformational states. Critical missing elements in the structural analysis of MetNIQ are the structure of the substrateā€free form of MetQ, and detailing how MetQ binds multiple methionine derivatives, including both Lā€ and Dā€methionine isomers. In this study, we report the structures of the Neisseria meningitides MetQ in substrateā€free form and in complexes with Lā€methionine and with Dā€methionine, along with the associated binding constants determined by isothermal titration calorimetry. Structures of the substrateā€free (N238A) and substrateā€bound N. meningitides MetQ are related by a ā€œVenusā€fly trapā€ hingeā€type movement of the two domains accompanying methionine binding and dissociation. Lā€methionine and Dā€methionine bind to the same site on MetQ, and this study emphasizes the important role of asparagine 238 in ligand binding and affinity. A thermodynamic analysis demonstrates that ligandā€free MetQ associates with the ATP bound form of MetNI ~40 times more tightly than does liganded MetQ, consistent with the necessity of dissociating methionine from MetQ for transport to occur

    Structures of the Neisseria meningitides methionineā€binding protein MetQ in substrate-free form and bound to L- and D-methionine isomers

    Get PDF
    The bacterial periplasmic methionineā€binding protein MetQ is involved in the import of methionine by the cognate MetNI methionine ABC transporter. The MetNIQ system is one of the few members of the ABC importer family that has been structurally characterized in multiple conformational states. Critical missing elements in the structural analysis of MetNIQ are the structure of the substrateā€free form of MetQ, and detailing how MetQ binds multiple methionine derivatives, including both Lā€ and Dā€methionine isomers. In this study, we report the structures of the Neisseria meningitides MetQ in substrateā€free form and in complexes with Lā€methionine and with Dā€methionine, along with the associated binding constants determined by isothermal titration calorimetry. Structures of the substrateā€free (N238A) and substrateā€bound N. meningitides MetQ are related by a ā€œVenusā€fly trapā€ hingeā€type movement of the two domains accompanying methionine binding and dissociation. Lā€methionine and Dā€methionine bind to the same site on MetQ, and this study emphasizes the important role of asparagine 238 in ligand binding and affinity. A thermodynamic analysis demonstrates that ligandā€free MetQ associates with the ATP bound form of MetNI ~40 times more tightly than does liganded MetQ, consistent with the necessity of dissociating methionine from MetQ for transport to occur
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