This course introduces and explains the physicochemical properties of biological macromolecules and their complexes, mostly in solution. The course offers an overview of protein and nucleic acid structures. Intra- and inter-molecular forces, helix-coil transitions and protein folding will be treated in a thermodynamical context.
This course is the second of the two-term biophysical chemistry series; however, it has been constructed to be a stand-alone course and can be taken without taking Biophysics 520. Biophysics 521 provides an overview of key methodologies of contemporary biophysics and biophysical chemistry. Principles of structure determination by X-ray diffraction, solution and solid-state NMR and electron microscopy will be covered. A variety of optical spectroscopic techniques, including UV/Vis, fluorescence, circular dichroism and cell imaging will be discussed. Methods for the separation and study of biological macromolecules and membranes including utracentrifugation, chromatography, electrophoresis, mass spectrometry and calorimetry will be introduced.
This course is team-taught by the following faculty: Ari Gafni, Hashim Al-Hashimi, Ayyalusamy Ramamoorthy, Giorgios Skiniotis and Janet Smith.
(This course is a meet-together with Biophysics 450)
This hands-on course teaches essential laboratory skills in Biophysics. Experiments cover sample preparation techniques, such as protein expression and purification; modern research methods such as atomic force microscopy, optical tweezers, NMR, X-ray crystallography, and computational techniques such as molecular dynamics simulation. The final project will allow students to explore a topic of interest in greater depth.
(This course is a meet-together with Biophysics 495)
This course teaches professional skills such as writing research articles, reviews, grant proposals, and preparing and giving poster presentations and scientific talks. The scientific publishing process, including peer review, will be discussed and ethical rules and considerations explored. All students will draft an application for an NSF Graduate Fellowship, which will be extensively critiqued by other students and the instructor.
Cross-listed with Biological Chemistry 602, Chemistry 602 and Pharmacology 602
In this course, students learn the theoretical and practical aspects of determining protein and nucleic structures by X-ray crystallography. The course will include topics such as crystallization, diffraction theory, phasing techniques and structure validation.
This course covers the fundamental physical and mathematical principles of microscopy. The emphasis is mainly on modern approaches, including superresolution fluorescence techniques and nonlinear microscopies. As well as teaching methods, the course will also extensively discuss their applications in biological/biochemical sciences. The physics and math level will assume some familiarity with geometrical and physical optics.
(Molecular Biophysics Training Grant students must enroll in Biophysics 801; all other students should enroll in Biophysics 802)
A weekly seminar where Biophysics students meet to discuss and present their research in a supportive peer setting.
Biophysics 890 — Intro to Research (1-4 credits)
First-year Biophysics students not in the PIBS program enroll in this course to obtain credit for their first two lab rotations.
Biophysics 990 — Diss-Precand (1-8 credits)
Biophysics pre-candidate students who have chosen a lab enroll in this course to obtain research credit.
Biophysics 995 — Diss-Cand (8 credits)
Biophysics candidate students enroll in this course to obtain research credit.