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Ranish lab published a preprint describing a new crosslinking mass spectrometry technology

Ranish Lab Proteins and Disease

Dynamic conformational and structural changes in proteins and protein complexes play a central and ubiquitous role in the regulation of protein function, yet it is very challenging to study these changes, especially for large protein complexes, under physiological conditions. To address this challenge, we created a novel isobaric crosslinker, Qlinker, for studying conformational and structural changes in proteins and protein complexes using quantitative crosslinking mass spectrometry (qCLMS).

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Ranish Lab Proteins and Disease
A new crosslinking mass spectrometry technology for studying conformational and structural changes in protein complexes

A new crosslinking mass spectrometry technology for studying conformational and structural changes in protein complexes

Our work describing a new crosslinking mass spectrometry technology for studying conformational and structural changes in proteins and proteins complexes has been published in eLife.

A new crosslinking mass spectrometry technology for studying conformational and structural changes in protein complexes
A new crosslinking mass spectrometry technology for studying conformational and structural changes in protein complexes

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Ranish Lab Proteins and Disease
A Better Understanding of DNA Unpacking

A Better Understanding of DNA Unpacking

Jie Luo and Jeff Ranish collaborated on a project to determine the molecular architecture of the NuA4/Tip60 co-activator complex. This protein complex functions to allow proper control of gene expression and DNA repair by allowing other proteins to access the DNA in the cell nucleus. The new information about the structure and function of TIP60 could provide insight into different diseases where the protein complex plays a role, such as Alzheimer’s and various cancers. The work was published in Science.

A Better Understanding of DNA Unpacking
A Better Understanding of DNA Unpacking

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Ranish Lab Proteins and Disease
Identification of key residues within p52/Tfb2 required for TFIIH function at transcription start sites in human and yeast cells

Identification of key residues within p52/Tfb2 required for TFIIH function at transcription start sites in human and yeast cells

Completing a years-long collaboration with the Taatjes and Kaplan labs, we publish an article in JBC that identifies key residues within the p52/Tfb2 subunit that control TFIIH function at transcription start sites in human and yeast cells.

Identification of key residues within p52/Tfb2 required for TFIIH function at transcription start sites in human and yeast cells
Identification of key residues within p52/Tfb2 required for TFIIH function at transcription start sites in human and yeast cells