Che-Fan Jeffrey Huang

@jfhorner.bsky.social

A Taiwanese in Chicago 👨‍🔬📯🌈🧋🧋🧋 Proteome explorer, horn player and boba enthusiast!

I will be presenting at Consortium for Top-Down Proteomics’s Proteoform Thursday Webinar Series. The catenin phospho-code work laid the foundation for my future research group. Free register link below!

Consortium for Top-Down Proteomics@proteoforms.bsky.social · 5mo ago

Join us March 26 for Proteoform Thursday: Jeffrey Huang presents - "A Catenin Phospho-Code for Adherens Junction Organization" us06web.zoom.us/meeting/regi... #proteomics #massspec

It was a great pleasure attending my first #HUPO world congress in Toronto last week and sharing our catenin phospho-code story! It was inspiring meeting with peers and pioneers in the field, which reminded me how special the proteomics community is!

BildBild

High-performance proteomics at any chromatographic flow rate These data follow the expected trends as though taken from a textbook ! They illustrate clearly the trade-offs between high and low flow rates.

Bild

The mass spectrometry research community at Chicago is thriving! Many thanks to the Chicago Mass Spec Interest Group for the invitation to share my catenin proteoform story in the inaugural event. It was a pleasure to meet with researchers at the beautiful CZbiohub space!

BildBildBildBild

Looking forward to attending the #USHUPO conference in Philly this weekend and sharing some early results in catenin proteoform profiling and our vision to build a story behind acto-myosin contractility regulation in cell-cell adhesion. Please join my talk next Wednesday and say hi!

Bild

New manuscript from the lab to establish a Top Down MS platform using electron activated dissociation on the Sciex ZenoTOF 7600 is out at the Journal of Proteome Research! pubs.acs.org/doi/full/10....

Establishing a Top-Down Proteomics Platform on a Time-of-Flight Instrument with Electron-Activated Dissociation

Top-down proteomics is the study of intact proteins and their post-translational modifications with mass spectrometry. Historically, this field is more challenging than its bottom-up counterpart because the species are much bigger and have a larger number of possible combinations of sequences and modifications; thus, there is a great need for technological development. With improvements in instrumentation and a multiplicity of fragmentation modes available, top-down proteomics is quickly gaining in popularity with renewed attention on increasing confidence in identification and quantification. Here, we systematically evaluated the Sciex ZenoTOF 7600 system for top-down proteomics, applying standards in the field to validate the platform and further experimenting with its capabilities in electron-activated dissociation and post-translational modification site localization. The instrument demonstrated robustness in standard proteins for platform QC, as aided by zeno trapping. We were also able to apply this to histone post-translational modifications, achieving high sequence coverage that allowed PTM’s site localization across protein sequences with optimized EAD fragmentation. We demonstrated the ability to analyze proteins spanning the mass range and included analysis of glycosylated proteins. This is a reference point for future top-down proteomics experiments to be conducted on the ZenoTOF 7600 system.

pubs.acs.org

Very happy to share my third major work this year (and first on 🦋)! This is a co-first work with the Fitzgerald group at Duke where they perform the SPROX protein folding stability assay and I figure out how to decribe the results using top-down proteomics! doi.org/10.1021/acs....

Top-Down Stability of Proteins from Rates of Oxidation (TD-SPROX) Approach for Measuring Proteoform-Specific Folding Stability

The crucial roles of proteoforms in biological processes and disease mechanisms have been increasingly recognized. However, the rate at which new proteoforms are being discovered using top-down proteomics has far outpaced the rate at which the functional significance of different proteoforms can be determined. Because of the close connection between protein folding and protein function, protein folding stability measurements on proteoforms have the potential to identify functionally significant proteoforms of a given protein. While a number of mass spectrometry-based proteomics methods for making protein folding stability measurements on the proteomic scale have been reported over the past decade, none have been interfaced with top-down proteomics. Described here is a top-down (TD) stability of proteins from the rates of oxidation (SPROX) approach for making proteoform specific folding stability measurements. This approach is validated using a mixture of three model proteins with well-characterized protein folding behavior by conventional SPROX as well as other more conventional biophysical techniques. The method is also used to evaluate the relative folding stabilities of the <30 kDa protein fraction isolated from an MCF-7 cell lysate. The relative folding stabilities of 150 proteoforms from 83 proteins were successfully characterized in the cell lysate analysis using the TD-SPROX approach.

doi.org

Is “proteomics approach” the same thing as “proteomic approach”? I was under the impression that you should always add the s at the end of -omics, even as an adjective because it’s part of the word to show that we’re measuring thousands of targets at once. But I see people using proteomic without s.