The recent revision of undergraduate curricular guidelines from the American Chemical Society Committee on Professional Training (ACS-CPT) has generated interest in examining new ways of organizing course sequences both for chemistry majors and for nonmajors. A radical reconstruction of the foundation-level chemistry curriculum is presented in which content has been reorganized into three sequences: structure, reactivity, and quantitation. It is proposed that these three areas represent fundamental aspects of chemistry that cross traditional domains and allow students to more quickly appreciate the breadth of the field. An overview of these sequences in the chemistry curriculum at CSB/SJU is described.

A one-semester, introductory chemistry course is described that develops a primarily qualitative understanding of structure−property relationships. Starting from an atoms-first approach, the course examines the properties and three-dimensional structure of metallic and ionic solids before expanding into a thorough investigation of molecules. In addition to bonding, geometry, molecular orbitals, and intermolecular attractions, other structural topics are included, such as stereochemistry, conformation, and factors that influence the strength of Brønsted acids. Where appropriate, related considerations in biochemistry are highlighted. The course provides a common basis to majors and nonmajors for further study in chemistry and also serves as a platform to illustrate a variety of topics of current research interest.

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A cohort program to increase retention of under-represented groups in chemistry was developed at the College of Saint Benedict/Saint John’s University. In particular, this program chose to emphasize early career mentoring and early access to research. This goal was chosen because research has been repeatedly shown to increase scientific identity resulting in increased retention of students in the STEM fields. Several elements of this program have been useful in preparing students to access research programs early in their college careers including a summer bridge program, career mentoring, advising, and a second year “research bootcamp” course.

A laboratory project for a first semester biochemistry course is described, which integrates the traditional classroom study of the structure and function of biomolecules with the laboratory study of these molecules using fluorescence spectroscopy. Students are assigned a specific question addressing the stability/function of lipids, proteins, or nucleic acids, and asked to design an experiment to answer the question using fluorescence methodologies. Students study phase equilibria and determine the critical micelle concentration of single chain amphiphiles, the melting point of multilamellar vesicles, and the melting points and thermodynamic constants (K eq , DG 0 , DH 0 and DS 0 ) for denaturation of ds-DNA and proteins. In addition, they examine binding properties of proteins. These laboratory experiments are designed to support student learning of the major themes of structure and function in the course.Keywords: Laboratory exercises, protein structure function and folding, nucleic acid structure function and processing, membrane assembly and vesicle trafficking.Fluorescence spectroscopy is an increasingly essential tool for the study of biomolecular properties. Steadystate fluorescence properties (emission intensity, excitation and emission wavelength maxima) are very sensitive to the environment of the fluorophore and are readily used to study complex biological processes such as molecular interactions, stability, structure, and function. Given its widespread application in the study of biomolecules, it is important to extend the study of fluorescence theory and its applications past physical or biophysical chemistry courses [1] to traditional biochemistry courses as well. Undergraduate students in biology and biochemistry often have qualitative exposure to fluorescence microscopy, but are offered little that would increase their understanding of the principles involved and of a myriad of additional applications.If understanding is enhanced by providing a ''need-toknow'' environment, then continual integration of fluorescence theory into course and application into laboratory would provide maximal opportunity for students to learn the science and utility of fluorescence. Previous methods to achieve integration of content or methodology in course and laboratory have ranged from project-based laboratories based on specific techniques/instrumentation [2-5], specific molecules/molecular systems [6][7][8][9], or the development of entirely new project-based biochemistry laboratory courses [10,11]. Many articles have been published concerning the use of fluorescence spectroscopy in undergraduate laboratories to study specific biomolecules [12][13][14][15][16][17][18], but none have addressed the concept of applying the technique more broadly to complement the course and its themes in general. Over the last six years, we have conducted a variety of experiments for a biochemistry laboratory project integrating experimental uses of fluorescence spectroscopy with the fundamental themes of structure and function pres...