Elihu C. Ihms
Biochemistry, Genetics and Molecular Biology · The Ohio State University
Publications
16
Citations
92
Est. group size
~2
Recurring co-author estimate
Active years
16
Publishing since 2009
This researcher studies how proteins made of multiple identical subunits (homo-oligomers) bind small molecules and change shape, using bacterial regulatory proteins like TRAP and Anti-TRAP as model systems. The work combines structural biology techniques, native mass spectrometry, and calorimetry to understand cooperative binding, where one binding event influences neighboring sites, and has also touched on antibody drug formulation stability. Research output has been modest and intermittent over the past decade, with work carried out in a small group.
Publication output has been low and irregular over the last decade, with sporadic single or few-paper years and no clear growth trend (averaging under one paper per year in the last five years).
Generated by claude-sonnet-5 from public bibliographic data · Jul 20, 2026
- Solution structure, dynamics and tetrahedral assembly of Anti-TRAP, a homo-trimeric triskelion-shaped regulator of tryptophan biosynthesis in Bacillus subtilis
Journal of Structural Biology X · 2024
- Solution structure, dynamics and tetrahedral assembly of Anti-TRAP, a homo-trimeric triskelion-shaped regulator of tryptophan biosynthesis in <i>Bacillus subtilis</i>
bioRxiv (Cold Spring Harbor Laboratory) · 2023
- Thermodynamic coupling between neighboring binding sites in homo‐oligomeric ligand sensing proteins from mass resolved ligand‐dependent population distributions
Protein Science · 2022
- Thermodynamic coupling between neighboring binding sites in homo-oligomeric ligand sensing proteins from mass resolved ligand dependent population distributions
bioRxiv (Cold Spring Harbor Laboratory) · 2022
- Population Distributions from Native Mass Spectrometry Titrations Reveal Nearest-Neighbor Cooperativity in the Ring-Shaped Oligomeric Protein TRAP
Biochemistry · 2020
- Population Distributions from Native Mass Spectrometry Titrations Reveal Nearest-Neighbor Cooperativity in the Ring-Shaped Oligomeric Protein TRAP
ChemRxiv · 2020
- Population Distributions from Native Mass Spectrometry Titrations Reveal Nearest-Neighbor Cooperativity in the Ring-Shaped Oligomeric Protein TRAP
ChemRxiv · 2020
- Increase in Solubility of Monoclonal Antibodies - Formulation Perspective and the “Magic” of Arginine
Biophysical Journal · 2019
- Predicting the Stability of Monoclonal Antibodies at High Concentration Formulations
Biophysical Journal · 2019
- Mechanistic Models Fit to Variable Temperature Calorimetric Data Provide Insights into Cooperativity
Biophysical Journal · 2017
- elihuihms/itcsimlib: Initial alpha release
Zenodo (CERN European Organization for Nuclear Research) · 2016
- Biophysical Journal×3
- bioRxiv (Cold Spring Harbor Laboratory)×2
- ChemRxiv×2
- Protein Science×1
- Biochemistry×1
- Chiwook Park
Biochemistry, Genetics and Molecular Biology · Purdue University West Lafayette
- Tsukasa Nakamura
Biochemistry, Genetics and Molecular Biology · Purdue University West Lafayette
- Jacob Verburgt
Biochemistry, Genetics and Molecular Biology · Purdue University West Lafayette
- Carol Beth Post
Biochemistry, Genetics and Molecular Biology · Purdue University West Lafayette
- Andrzej Kloczkowski
Biochemistry, Genetics and Molecular Biology · The Ohio State University
This profile was generated automatically from public scholarly data (OpenAlex). Group size and activity levels are estimates derived from co-authorship patterns.
Last updated Jul 19, 2026.
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