Current Research

We plan to nurture and develop a group of well-trained, research-ready undergraduates who have a passion for science, the desire to engage in biomedical research careers and the ability to inspire peers to follow the same path.

Certain cohorts of the U.S. population do not contribute proportionately to biomedical research. Increasing the participation of these currently underrepresented minority (URM) groups is critical to draw from our full potential of scientific talent and to foster a sustainable pool of biomedical researchers for the future. URM students with insufficient educational backgrounds are often derailed early from scientific careers due to poor performance in introductory physical science courses.

At Cornell we have developed a pre-freshman preparatory (PSP) program to provide disadvantaged students supplemental training in quantitative thinking so that they can succeed in general chemistry courses. The PSP is based on intense problem-solving exercises and peer-led learning. A balance of problem types that encourage the development of physical intuition and general chemical reasoning provide the most effective outcomes.

Students participating in the PSP not only have greater success in freshman chemistry, but also show improvement in sophomore chemistry courses. Nonetheless, to encourage these students to ultimately pursue careers in research and medicine they require a second bridge. The first phase of this bridge will involve a pre-sophomore organic/biochemistry preparatory course based on the PSP model coupled with an initiation into laboratory work. In the second phase, students will conduct independent research over one summer in a mentored environment. As a group they will receive instruction in work practice, professional development, responsible conduct and hone their writing and presentation skills.

In addition, the students will lead scientific outreach efforts to K-12 schools from their originating communities through remote learning platforms that can be readily disseminated through electronic media. Finally, we have implemented the successful training methods of the PSP in two new companion courses to General Chemistry, which are made available in the regular academic year to any Cornell undergraduate. Our overall goal is to nurture a group of well-trained, research ready undergraduates who have a passion for science, the desire to engage in research careers and the ability to inspire peers to follow the same path.

Research Summary

The Crane group studies the chemistry underlying the transmission of signals in biological systems. We are particularly interested in poorly understood sensing mechanisms, such those involving light signaling, reactions of unstable intermediates, and conformational changes within large molecular assemblies. We have determined structures and assembly states of key proteins that comprise the signaling networks of bacterial chemotaxis and eukaryotic circadian clocks. In the former case, we are particularly interested in the transmembrane receptor arrays that direct bacterial motility.

We have characterized a novel family of chemotaxis phosphatases that includes an important element of the bacterial flagella motor; this work led to investigations of the motor itself, and includes the elucidation of a mechanism for the switching of rotor rotation. Our studies of circadian rhythms aim to understand how light entrains the central circadian oscillators of fungal and animal clocks. To this end we study molecular interactions within the oscillators and proteins involved in photo-entrainment.

In our studies of biological nitric oxide chemistry, we have described structures and intermediates in NO production by nitric oxide synthases and demonstrated novel roles for NO in bacterial physiology, which include the radiation resistance of extremophiles. Electron transfer reactions within proteins underlie many of processes we investigate. Thus, we are interested in the bonding networks and conformations that enable electron transfer over long distances and across protein interfaces. We approach these varied problems with a range of experimental techniques that include x-ray diffraction, solution scattering, time-resolved optical spectroscopy, dipolar ESR spectroscopy, enzymology, bacterial genetics and methods that monitor photochemical reactions in crystals.

As of March 10, 2015

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