Corie Ralston

Biochemist Staff Scientist
Facility Director, Biological Nanostructures, Molecular Foundry

Molecular Biophysics and Integrated Bioimaging

Structural Biology

Building: 6, Room 2128
Mail Stop: 6R2100
Phone: (510) 495-2594
CYRalston@lbl.gov

Curriculum Vitae

Research Interests

Beamline instrumentation, macromolecular crystallography and X-ray footprinting technique development.

LinkedIn Profile
ResearchGate Profile

Was this page useful?

Send

Kerfeld to Lead New DOE-funded Center for Catalysis in Biomimetic Confinement

December 15, 2022

With $10.65 million in support from the U.S. Department of Energy (DOE), a new Energy Frontier Research Center based at Michigan State University (MSU) has been established. Led by Cheryl Kerfeld, a professor in the MSU-DOE Plant Research Laboratory, the Center for Catalysis in Biomimetic Confinement (CCBC) will explore how nature compartmentalizes some of its most important biochemical reactions.

Congratulations to Biosciences Area Director’s Award Recipients

October 19, 2022

Each year, the Berkeley Lab Director’s Achievement Award program recognizes outstanding contributions by employees to all facets of Lab activities. Several Biosciences Area personnel are among the 2022 honorees.

Get a Move On: Protein Translates Chemistry into Motion

December 9, 2020

The protein CheY plays a role in relaying sensory signals from chemoreceptors to the rotary motor at the base of the tail-like appendage, or flagellum, that protrudes from the cell body of certain bacteria and eukaryotic cells. It has been studied as a model for dissecting the mechanism of allostery—the process by which the binding of biological macromolecules (mainly proteins) at one location regulates activity at another, often distant, functional site. When it is transiently phosphorylated in response to chemotactic cues, CheY’s binding affinity for a flagellar motor switch protein called FliM is enhanced. CheY binding to FliM changes the direction of flagellar rotation from counterclockwise to clockwise.

Using X-ray footprinting with mass spectroscopy (XFMS), a team led by Shahid Khan, a senior scientist with the Molecular Biology Consortium, established that CheY changes shape when it tethers to the motor, and further parsed the contribution of phosphorylation to this shape change. The results of the XFMS experiments validated atomistic molecular dynamics (MD) predictions of the architecture of the allosteric communication network, marking the first time that XFMS has been used to validate protein dynamics simulations at single-residue resolution sampled over the complete protein.

Research Interests

About Biosciences

Divisions & User Facility

Resources