Graduate College Climate Survey

The purpose of this survey is to assess the diverse climate of graduate students’ experiences at ISU. The retention and persistence of graduate students at ISU continues to be an ongoing topic of conversation within the graduate college and academic departments. Graduate students play an integral role in research and scholarship on campus and it is critical that the department and lab climate foster a positive environment for all graduate students at ISU. In an unhealthy climate, students are less likely to adjust academically and are less likely to develop a sense of belonging on the campus. Assessing campus climate and then taking action to create and sustain a healthy climate are essential steps to creating an environment that supports the fundamental mission of the university —teaching, research, and service. Addressing climate benefits all campus community members, not just historically underrepresented students, faculty and staff. Our aims are to provide an outlet for graduate students to share their experiences within departments, bring awareness of climate issue, and equip faculty, staff and students with the skills and tools need to address current and future problems

The normative value orientations of collaborative entrepreneurs

Includes bibliographical referencesAvailable from British Library Document Supply Centre- DSC:D222422 / BLDSC - British Library Document Supply CentreSIGLEGBUnited Kingdo

Graduate College Climate Survey

The purpose of this survey is to assess the diverse climate of graduate students’ experiences at ISU. The retention and persistence of graduate students at ISU continues to be an ongoing topic of conversation within the graduate college and academic departments. Graduate students play an integral role in research and scholarship on campus and it is critical that the department and lab climate foster a positive environment for all graduate students at ISU. In an unhealthy climate, students are less likely to adjust academically and are less likely to develop a sense of belonging on the campus. Assessing campus climate and then taking action to create and sustain a healthy climate are essential steps to creating an environment that supports the fundamental mission of the university —teaching, research, and service. Addressing climate benefits all campus community members, not just historically underrepresented students, faculty and staff. Our aims are to provide an outlet for graduate students to share their experiences within departments, bring awareness of climate issue, and equip faculty, staff and students with the skills and tools need to address current and future problems.</p

Mg 2+

Thymidylate synthase (TSase) produces the sole intracellular de novo source of thymidine (i.e. the DNA base T) and thus is a common target for antibiotic and anticancer drugs. Mg(2+) has been reported to affect TSase activity, but the mechanism of this interaction has not been investigated. Here we show that Mg(2+) binds to the surface of Escherichia coli TSase and affects the kinetics of hydride transfer at the interior active site (16 Å away). Examination of the crystal structures identifies a Mg(2+) near the glutamyl moiety of the folate cofactor, providing the first structural evidence for Mg(2+) binding to TSase. The kinetics and NMR relaxation experiments suggest that the weak binding of Mg(2+) to the protein surface stabilizes the closed conformation of the ternary enzyme complex and reduces the entropy of activation on the hydride transfer step. Mg(2+) accelerates the hydride transfer by ca. 7-fold but does not affect the magnitude or temperature-dependence of the intrinsic kinetic isotope effect. These results suggest that Mg(2+) facilitates the protein motions that bring the hydride donor and acceptor together, but it does not change the tunneling ready state of the hydride transfer. These findings highlight how variations in cellular Mg(2+) concentration can modulate enzyme activity through long-range interactions in the protein, rather than binding at the active site. The interaction of Mg(2+) with the glutamyl-tail of the folate cofactor and nonconserved residues of bacterial TSase may assist in designing antifolates with poly-glutamyl substitutes as species-specific antibiotic drugs