S1 hydrophobic residues modulate voltage sensing phosphatase enzymatic function and voltage sensing.

The voltage sensing domain (VSD) is a four-helix modular protein domain that converts electrical signals into conformational changes, leading to open pores and active enzymes. In most voltage sensing proteins, the VSDs do not interact with one another and the S1-S3 helices are considered mainly as scaffolding. The two exceptions are the voltage sensing phosphatase (VSP) and the proton channel (Hv).

Perceptions of narcissism in college professors.

We conducted three studies to examine perceptions of grandiose narcissism in college professors. Narcissism might appear incompatible with the profession if professors are viewed fundamentally as helpers or as introverted bookworms. Then again, people might expect professors to display big egos congruent with the prestige of their profession and their privileged public platforms.

Research capacity-building program for clinicians and staff at a community-based HIV clinic in Uganda: A pre/post evaluation.

Developing capacity for HIV research and clinical practice is critically needed in resource-limited countries. The purpose of this study was to evaluate a research capacity-building program for community-based participants in the preparation and conduct of mobile phone-based technology interventions. A descriptive, cross-sectional design was used.

A comparison of stigmatellin conformations, free and bound to the photosynthetic reaction center and the cytochrome bc1 complex.

We describe in detail the conformations of the inhibitor stigmatellin in its free form and bound to the ubiquinone-reducing (Q(B)) site of the reaction center and to the ubiquinol-oxidizing (Q(o)) site of the cytochrome bc(1) complex. We present here the first structures of a stereochemically correct stigmatellin in complexes with a bacterial reaction center and the yeast cytochrome bc1 complex. The conformations of the inhibitor bound to the two enzymes are not the same.