Wednesday Nite at the Lab
press release: For the fall semester, WN@TL goes hybrid both with Zoom and with in-person (Room 1111) presentations. The zoom registration link is still go.wisc.edu/240r59. You can also watch a live web stream at biotech.wisc.edu/webcams
On June 15 Kenny Lee of the Joshua Coon Lab in Biochemical Sciences and the Morgridge Institute speaks on “Studying Protein Structures in a Space-like Environment: Integration of Mass Spectrometry and Electron Microscopy for Structural Biology.”
Description: Structural biology focuses on correlating biomolecular structure to function. It is known that proteins take specific shapes and self-assemble into larger complexes with other molecules to perform vital roles. With the development of powerful tools such as NMR spectroscopy, X-ray crystallography, and electron microscopy, scientists have uncovered many structures and shown how their three-dimensional shapes influence their cellular functions. Mass spectrometry has more recently gained traction in the field of structural biology as a complementary approach. Whereas careful measurements with crystallography and microscopy generate detailed three-dimensional images, mass spectrometry provides important molecular information such as the number of individual components in a large complex and their individual masses.
One strength of mass spectrometry is its ability to weigh and sort different components in a mixture; however, this requires the molecules in the sample to be removed from their stable liquid environment and suspended in electric fields under high vacuum as highly charged particles. We use a technique called electrospray ionization to gently apply charge to the molecules and transfer them into the vacuum environment of the mass spectrometer, but whether these molecules retained their native liquid-phase structure remained a question. An approach termed “soft-landing” can address this question by transmitting the charged molecules through the mass spectrometer and collecting them on a surface. The landed particles can then be imaged with electron microscopy.
Our contributions to the soft-landing experiment have increased the quality and quantity of landed particles such that we published the first 3D reconstruction of a protein complex that had traveled through a mass spectrometer. This result demonstrated that stable biomolecular structures remain intact as highly charged particles under high vacuum. We aim to further develop soft-landing via mass spectrometry followed by analysis with electron microscopy as a hybrid structural biology tool to characterize biomolecular structures that are typically difficult to study because of low amounts or sample complexity.
Bio: Kenny earned his B.S. in Chemistry at Brigham Young University and his PhD in Chemistry at Purdue University. At Purdue, he learned the fundamentals of mass spectrometry instrumentation while developing electronics and hardware to perform measurements on large biomolecular structures for a home-built mass spectrometer. He is currently a postdoctoral researcher in the Coon lab at UW-Madison where he is continuing to develop mass spectrometry instrumentation for multiple biological applications and working in a team that is interfacing mass spectrometry with electron microscopy as a novel approach to studying biomolecular structure. He lives with his wife Tashina and their 18-month-old daughter Violet in east Madison.
Explore More:
Game-changer: New tech could transform biotechnology - Morgridge Institute for Research
Native Mass Spectrometry: A Glimpse Into the Machinations of Biology | Technology Networks
-=-=
Google
Yahoo
Outlook
ical