Author

H. T. Hobbs

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 2 Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 3 Organism:E. coli· 1 Research Focus:host-pathogen & immune response· 1 Assay:protein structure· 1 Assay:proteomics· 1 Approach:statistical model· 1 Assay:structural biology· 1

Frequent Co-Authors

S. Marqusee· 4 shared J. Kuriyan· 2 shared N. H. Shah· 2 shared S. R. Shoemaker· 2 shared A. Glasgow· 1 shared A. W. Nguyen· 1 shared C. L. Gee· 1 shared C.-L. Hsieh· 1 shared

Activity by Year

2021-2022 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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4 shared papersBiochemistry

S. Marqusee

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Author profile →

4 papers

Recent·Most cited

Saturation mutagenesis of a predicted ancestral Syk-family kinase

H. T. Hobbs, N. H. Shah, S. R. Shoemaker, J. F. Amacher, S. Marqusee, J. Kuriyan

The paper generates a bacterial-expressible Syk-family kinase via ancestral sequence reconstruction and uses deep mutational scanning to identify functional mutations.

bioRxiv · Apr 24, 2022Biochemistry

Ligand-induced changes in dynamics mediate long-range allostery in the lac repressor

A. Glasgow, H. T. Hobbs, Z. R. Perry, S. Marqusee, T. Kortemme

This study uses HDX/MS to show ligand-induced changes in dynamics mediate long-range allostery in the lac repressor, revealing flexibility differences in secondary structures across functional states.

bioRxiv · Nov 30, 2021Biophysics

Differences in the dynamics of the tandem-SH2 modules of the Syk and ZAP-70 tyrosine kinases

H. T. Hobbs, N. H. Shah, J. M. Badroos, C. L. Gee, S. Marqusee, J. Kuriyan

This study compares the conformational dynamics of the tandem-SH2 modules in Syk and ZAP-70 kinases, revealing differences in their autoinhibited states and activation mechanisms.

bioRxiv · Jul 20, 2021Biochemistry

The SARS-CoV-2 spike reversibly samples an open-trimer conformation exposing novel epitopes

S. M. Costello, S. R. Shoemaker, H. T. Hobbs, A. W. Nguyen, C.-L. Hsieh, J. A. Maynard, J. S. McLellan, J. E. Pak, S. Marqusee

The paper identifies an alternative open-trimer conformation of the SARS-CoV-2 spike ectodomain that exposes novel epitopes and is modulated by temperature, binding, and sequence variants.

bioRxiv · Jul 11, 2021Biophysics