
Gerwald Jogl
· Associate Professor of BiologyBrown University · Genetics
Active 1997–2026
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About
Gerwald Jogl is an Associate Professor of Biology with a background in Chemistry, holding a Ph.D. from the University of Graz, Austria. His doctoral research involved X-ray and Neutron Diffraction Studies of B12 Coenzymes in both free and enzyme-bound states. He has also completed post-doctoral research as a Research Associate with Liang Tong at Columbia University. His research areas include structural biology, cryo-electron microscopy, antibiotic resistance, CRISPR-Cas activation, retrotransposons, and ribosome function. Jogl's work involves detailed structural and biochemical studies of various biological molecules, including ribosomal components, enzymes involved in biosynthesis, and elements of the CRISPR system, contributing to a deeper understanding of molecular mechanisms and potential therapeutic targets.
Research topics
- Biology
- Computational biology
- Chemistry
- Geometry
- Microbiology
- Organic chemistry
- Mathematical analysis
- Biophysics
- Physics
- Mathematics
Selected publications
Phase separation of the LINE-1 ORF1 protein is mediated by the N-terminus and coiled-coil domain
Biophysical Journal · 2021 · 56 citations
Senior authorCorrespondingHigh-fidelity, hyper-accurate, and evolved mutants rewire atomic-level communication in CRISPR-Cas9
Science Advances · 2024-03-06 · 42 citations
articleOpen accessThe high-fidelity (HF1), hyper-accurate (Hypa), and evolved (Evo) variants of the CRISPR-associated protein 9 (Cas9) endonuclease are critical tools to mitigate off-target effects in the application of CRISPR-Cas9 technology. The mechanisms by which mutations in recognition subdomain 3 (Rec3) mediate specificity in these variants are poorly understood. Here, solution nuclear magnetic resonance and molecular dynamics simulations establish the structural and dynamic effects of high-specificity mut…
Cryo-electron microscopy structure of the 70S ribosome from Enterococcus faecalis
Scientific Reports · 2020 · 29 citations
Senior authorCorrespondingEnterococcus faecalis is a gram-positive organism responsible for serious infections in humans, but as with many bacterial pathogens, resistance has rendered a number of commonly used antibiotics ineffective. Here, we report the cryo-EM structure of the E. faecalis 70S ribosome to a global resolution of 2.8 Å. Structural differences are clustered in peripheral and solvent exposed regions when compared with Escherichia coli, whereas functional centres, including antibiotic binding sites, are simi…
Structural and dynamic insights into the HNH nuclease of divergent Cas9 species
Journal of Structural Biology · 2021-12-03 · 22 citations
articleOpen accessThe Journal of Chemical Physics · 2022-12-14 · 17 citations
articleOpen accessAllosteric signaling within multidomain proteins is a driver of communication between spatially distant functional sites. Understanding the mechanism of allosteric coupling in large multidomain proteins is the most promising route to achieving spatial and temporal control of the system. The recent explosion of CRISPR-Cas9 applications in molecular biology and medicine has created a need to understand how the atomic level protein dynamics of Cas9, which are the driving force of its allosteric cro…
Recent grants
NIH · $9.0M · 2012
Structural Robustness of Ribosome Functional Centers
NIH · $4.4M · 2010–2026
NIH · $17.2M · 2013
Frequent coauthors
- 56 shared
Steven T. Gregory
University of Rhode Island
- 55 shared
George P. Lisi
Providence College
- 54 shared
Alexandra M. D’Ordine
Providence College
- 48 shared
Albert E. Dahĺberg
Providence College
- 46 shared
Hasan DeMi̇rci̇
Koç University
- 39 shared
Helen B. Belato
Providence College
- 25 shared
Jinping Luo
Providence College
- 22 shared
E. Murphy
Providence College
Labs
Gerwald Jogl LaboratoryPI
Education
Ph.D., Chemistry
University of Graz, Austria
M.S., Chemistry
University Graz, Austria
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