Author

C. H. Trinh

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· 1 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Approach:biophysical modeling· 1 Research Focus:cell type annotation· 1 Research Focus:drug response / drug discovery· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Assay:proteomics· 1

Frequent Co-Authors

A. J. Wilson· 2 shared B. I. Wicky· 1 shared B. R. Jackson· 1 shared C. Ottmann· 1 shared C. Tiede· 1 shared D. C. Tomlinson· 1 shared F. A. Nadat· 1 shared F. Hobor· 1 shared

Activity by Year

2019-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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2 shared papersBiophysics

A. J. Wilson

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2 papers

Recent·Most cited

Understanding the interaction of 14-3-3 proteins with hDMX and hDM2: a structural and biophysical study

S. Srdanovic, M. Wolter, C. H. Trinh, C. Ottmann, S. L. Warriner, A. J. Wilson

The paper investigates the structural and biophysical interactions between 14-3-3 proteins and hDMX/hDM2, identifying key phosphosites that enable high-affinity binding.

bioRxiv · Dec 17, 2021Biophysics

Selective Affimers Recognize BCL-2 Family Proteins Through Non-Canonical Structural Motifs

T. A. Edwards, J. A. Miles, F. Hobor, J. L. Taylor, C. Tiede, P. L. Rowell, C. H. Trinh, B. R. Jackson, F. A. Nadat, H. F. Kyle, B. I. Wicky, J. Clarke, D. C. Tomlinson, A. J. Wilson

The paper identifies Affimer reagents that selectively bind BCL-2 family proteins through non-canonical structural motifs, showing competitive inhibition and conformational changes.

bioRxiv · May 27, 2019 · PreprintBiochemistry