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Lab Members

Graduate Students


Stephanie Breunig

Chemistry

Office: 332 Spalding Laboratory

MC 210-41

Office Phone: 2508

sbreunig AT caltech.edu

 

Stephanie

I am interested in using chemical tools to develop novel proteins with interesting and useful properties.


Samuel Ho

Chemistry

Office: 327 Spalding Laboratory

MC 210-41

Office Phone: 2508

samuelho AT caltech.edu

 

sammmmm

Super-resolution microscopy for dynamic imaging of bacterial proteins in-vivo.


Mark Kozlowski

Chemistry

Office: 309 Spalding Laboratory

MC 210-41

Office Phone: 2509

mtk AT caltech.edu

 

I develop strategies for constructing microbial communities, as well as make protein-based materials for pancreatic progenitor cell differentiation.


Hanwei Liu

Chemistry

Office: 327 Spalding Laboratory

MC: 210-41

Office Phone: 2508

hliu2 AT caltech.edu

 

I am working on creating living materials based on bacteria which can secrete different engineered protein based on stimuli the material receives


 

Xinran Liu

Chemical Engineering

Office: 327 Spalding Laboratory

MC 210-41

Office Phone: 2508

xlliu AT caltech.edu

 

I am interested in using bio-orthogonal amino acid tagging (BONCAT) to target nutrient-limited cells in biofilms and link a known physiological state to the labeled subpopulation's proteomic profile.


Xinyan Liu

Chemical Engineering

Office: 309 Spalding Laboratory

MC 210-41

Office Phone: 2510

xliu3 AT caltech.edu

 

I am interested in deploying bio-orthogonal non-canonical amino acid tagging (BONCAT) as a tool to study the bacterial phenotypic heterogeneity from isogenic populations and understanding bacterial persistence.


 

Elliot MacKrell

Chemical Engineering 

Office: 311 Spalding Laboratory

MC 210-41 

Office Phone: 2510 

emackrel AT caltech.edu

   Elliot
I am developing mutant aminoacyl-tRNA synthetases for characterizing transient cellular states with bioorthogonal noncanonical amino acid tagging (BONCAT).

Sophie Miller

Chemical Engineering

Office: 311 Spalding Laboratory

MC 210-41

Office Phone: 2510

semiller AT caltech.edu

 

I investigate local translation of proteins in neurons using fluorescence microscopy to detect interactions between RNAs.

Maiko Obana

Chemistry

Office: 311 Spalding Laboratory

MC 127-72

Office Phone: 2508

mobana AT caltech.edu

 

I am interested in the design of protein-based biomaterials by genetic engineering and self-assembly. My research focuses on the control of colloidal assembly by associative protein such as coiled-coil domains, towards the genetically encoded assembly of robust microbial communities.


Bradley Silverman

Chemical Engineering

Office: 309 Spalding Laboratory

MC 210-41

Office Phone: 2509

bsilverm AT caltech.edu

 

I'm interested in genetic programming of spatial organization of microbial communities for applications in studying the GI tract and in building complex bioreactors.


Shannon E. Stone

Chemistry

Office: 327 Spalding Laboratory

MC 210-41

Office Phone: 2508

stone AT caltech.edu

 

I am using bio-orthogonal non-canonical amino acid tagging (BONCAT) to discover proteins involved in host-pathogen interactions. Cell-selective labeling allows for enrichment of the few bacterial proteins present among the abundant host ones. By studying the proteins made during active infection, we may be able to discover new antibiotic targets.


 

Postdoctoral Fellows

 

Joshua Baccile

Chemistry

Office: 309 Spalding Laboratory

MC 210-41

Office Phone: 2509

baccile AT caltech.edu

 

 

My research aims to develop methods that enable sequence directed optimization of protein-based biomaterials used for 3D cell culture and establish general design principles for these and other materials used in tissue engineering.

Alex Chapman

Chemistry

Office: 311 Spalding Laboratory

MC 210-41

Office Phone: 2508

amchapma AT caltech.edu

 

I am interested in using residue- and site-specific incorporation of unnatural amino acids into therapeutically relevant proteins towards the goal of identifying improved protein drug leads, as well as to study modes of action that may not be achievable using the standard set of 20 amino acids.