Refinement of protein Fe(II) binding characteristics utilizing a competition assay exploiting small molecule ferrous chelators.

Iron is the most prevalent metal in biology. Its chemical and redox versatility allows it to direct activity of many Fe binding proteins. While iron's biological applications are diverse, challenges inherent in having Fe(II) present at high abundance means cells must ensure delivery to the correct recipient, while also ensuring its chemistry is regulated.

Great expectations: using an analysis of current practices to propose a framework for the undergraduate inorganic curriculum.

The undergraduate inorganic chemistry curriculum in the United States mirrors the broad diversity of the inorganic research community and poses a challenge for the development of a coherent curriculum that is thorough, rigorous, and engaging. A recent large survey of the inorganic community has provided information about the current organization and content of the inorganic curriculum from an institutional level. The data reveal shared "core" concepts that are broadly taught, with tremendous variation in content coverage beyond these central ideas.

Inorganic chemistry and IONiC: an online community bringing cutting-edge research into the classroom.

This Viewpoint highlights creative ways that members of the Interactive Online Network of Inorganic Chemists (IONiC) are using journal articles from Inorganic Chemistry to engage undergraduate students in the classroom. We provide information about specific educational materials and networking features available free of charge to the inorganic community on IONiC's web home, the Virtual Inorganic Pedagogical Electronic Resource (VIPEr, www.ionicviper.

Blood pressure and bone mineral density in premenopausal and postmenopausal women.

Introduction: Previous studies regarding the associations between blood pressure (BP) and bone mineral density (BMD) have shown conflicting results. However, menopausal status and pharmacotherapy may modify this relationship. The objective of this study was to explore the association between systolic BP (SBP) and diastolic BP (DBP) and BMD in pre- and postmenopausal women, and to assess the extent to which this association is mediated by menopausal status and pharmacotherapy.

Association of Copper to Riboflavin Binding Protein; Characterization by EPR and XAS.

The association of copper to Riboflavin Binding Protein (RBP) from egg white has been studied by electron paramagnetic resonance (EPR) and X-ray absorption (XAS) spectroscopies. The type II site contains a mix of copper I and II in an oxygen rich environment.

Gastroenterologists' prescribing of infliximab for Crohn's disease: a national survey.

Background: Practice guidelines suggest that immunomodulators (IMs) be given prior to infliximab (IFX) in patients with Crohn's disease (CD). The package insert for IFX recommends that maintenance therapy be prescribed for patients who respond to induction therapy. Our aim was to determine the extent to which gastroenterologists (GIs) are utilizing IM prior to IFX and prescribing maintenance IFX when treating patients with CD.

Investigation of the copper binding site and the role of histidine as a ligand in riboflavin binding protein.

Riboflavin Binding Protein (RBP) binds copper in a 1:1 molar ratio, forming a distinct well-ordered type II site. The nature of this site has been examined using X-ray absorption and pulsed electron paramagnetic resonance (EPR) spectroscopies, revealing a four coordinate oxygen/nitrogen rich environment. On the basis of analysis of the Cambridge Structural Database, the average protein bound copper-ligand bond length of 1.

Riboflavin binding protein contains a type II copper binding site.

Riboflavin binding protein, purified from egg white, binds copper(II) under dialysis conditions in an approximately 1:1 molar ratio. Results further indicate a small, but not negligible, amount of copper is present in the protein as purified from egg white. Electron paramagnetic resonance indicates a single type II copper site present in the protein.