Chris Petzold

Biochemist Staff Scientist

Process Engineering & Analytics

Building: 978, Room 4256
Mail Stop: 978-4121
Phone: (510) 486-7237
CJPetzold@lbl.gov
http://www.jbei.org/people/directors/chris-petzold/

Curriculum Vitae

Research Interests

Bioanalytical Mass Spectrometry, Proteomics, Analytical Chemistry, Metabolic Engineering

Selected Publications
Selected Publications

LinkedIn Profile
ResearchGate Profile

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Biomanufacturing Increases Available Supply of Anti-cancer Drug

September 1, 2022

The supply of a plant-derived anti-cancer drug can finally meet global demand after a team of scientists from Denmark and the U.S. engineered yeast to produce the precursor molecules, which could previously only be obtained in trace concentrations in the native plant. A study describing the breakthrough was recently published in Nature. The international team included four researchers from the Biological Systems and Engineering Division: Leanne Jade G. Chan, Edward Baidoo, Christopher J. Petzold, and Jay D. Keasling.

New Protein Functions from Beneficial Human Gut Bacterium

March 8, 2021

Researchers in the Environmental Genomics and Systems Biology (EGSB) and Biological Systems and Engineering (BSE) Divisions at Berkeley Lab employed a large-scale functional genomics approach to systematically characterize Bacteroides thetaiotaomicron, a beneficial bacterium prevalent in the human gut. They performed hundreds of genome-wide fitness assays and identified new functions for 40 proteins, including antibiotic tolerance, polysaccharide degradation, and colonization of the GI tract in germ-free mice.

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.

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