Structural Biology & Biophysics Facilities

Research Labs

About Our Research Labs

Research in Structural Biology & Biophysics is world-class, as evidenced by the large number of publications, and research grants awarded to Faculty members in this area. Some of the most important challenges facing mankind today, such as understanding Alzheimers Disease and the evolution of "superbugs" resistant to antibiotics, are being studied in our laboratories. The latest hardware, the vast knowledge base of research group members, and the stimulating and challenging environment created for graduate students by the BMBB PhD Program, enables students to tackle whatever biological questions pose themselves during the formulation of their thesis.

Weekly Structural Biology Club meetings provide a forum for students to present their research, listen and talk with visiting researchers and interact with other research lab members. Other opportunities for interaction come from more focused group meetings, such as those organized by the NMR users group and the Center for Metals in Biocatalysis.

Research facilities

Electron Paramagnetic Resonance

Electron Paramagnetic Resonance is a powerful, versatile, nondestructive and nonintrusive analytical method. EPR can yield meaningful structural and dynamical information, even from ongoing chemical or physical processes without influencing the process itself. Conventional EPR can be used to measure orientation and rotational motions in the time range from picoseconds to nanoseconds, while saturation transfer EPR extends this to the microsecond time scale. Site-directed spin labeling (SDSL), in which Cys mutagenesis is used to place Cys-reactive spin labels at desired sites on a protein, can be used to determine protein secondary and tertiary structure, and to measure structural changes that are inaccessible to conventional structural techniques.

Laser Spectroscopy (Optical)

The Laser Spectroscopy Laboratory in the Division of Structural Biology and Biophysics, is a shared resource (operated as an ISO) that contains instrumentation for time resolved fluorescence (picoseconds to nanoseconds) and phosphorescence (microseconds to milliseconds) experiments. These experiments are used for analyzing protein and lipid dynamics and association.

* Fluorescence: ISS K2 Multifrequency Time-Resolved Fluorometer, using a high-power Ar laser.

* Phosphorescence: Time resolved detection of emission or absorption following a pulse from a XeCl excimer laser.

Muscle Mechanics

Single fibers from rabbit, rat, and scallop muscles are studied on this instrument to determine their mechanical properties. We are able to simultaneously measure maximal isometric force generation (how "strong" the muscle fibers are) and myosin ATPase activity (rate of "energy" used before and during a contraction), as illustrated in the figure at right. On other instruments we are also able to determine maximal shortening velocity (how "fast" fibers can contract) and maximal power output (how "powerful" fibers are) of single muscle fibers.

Nuclear Magnetic Resonance

Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool for studying protein structure and dynamics, and for characterizing molecular interactions. The NMR facility at the University of Minnesota ranks among the best in the world and the research of four different groups in the BMBB department is dedicated to using NMR spectroscopy to solve biological problems. Please visit our NMR web page and view our fine facility.




X-Ray Crystallography

The Kahlert Structural Biology Laboratory (KSBL)

The biological molecules that make up our bodies have evolved exquisite ways to control and promote complex chemistries and communications that orchestrate our daily lives, as well as keep harmful disease causing “bugs” at bay. When these systems malfunction, or the immune system is overwhelmed, the effects can be catastrophic.

To understand the changes that lead to adverse effects to human health and also disease, we need to understand how the molecular “players” work. Most drugs and toxic compounds are small relative to the biological molecules they target. We therefore need to image the interactions on the scale of these smaller compounds. One of the major routes to obtaining highly detailed images of biological molecules at the level of the compounds to which they bind, is using a technique called X-ray crystallography. Results using this technique have impacted human health and disease in many ways. Improving drug efficacy and selectivity (reducing unwanted side-effects) through improved design; guiding vaccine development; understanding the evolution of multi-drug resistant organisms, and how to combat them; optimization of strategies for the removal of toxic compounds from the environment; engineering bacteria into factories for complex drug production.