Author

P. P. Samuel

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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Biophysics· 2

Signature Assays, Organisms & Methods

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Organism:human· 2 Research Focus:protein folding & dynamics· 2 Approach:statistical model· 2 Assay:proteomics· 1 Assay:structural biology· 1

Frequent Co-Authors

D. A. Case· 1 shared G. N. Phillips· 1 shared J. S. Olson· 1 shared M. A. White· 1 shared M. Gruebele· 1 shared M. M. Rickard· 1 shared T. V. V. Pogorelov· 1 shared W. C. Ou· 1 shared

Activity by Year

2020-2022 · peak 1/yr

Co-Author Collaboration Network

8 top collaborators · 13 mutual co-author links

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1 shared paperBiophysics

D. A. Case

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2 papers

Recent·Most cited

BiophysicsbioRxivPreprintSep 13, 2022

Metabolons, quinary structure, and domain motion: enzyme choreography in the cytoplasm

P. P. Samuel, M. M. Rickard, T. V. V. Pogorelov, M. Gruebele

The paper simulates a human cytoplasm model to study metabolon formation, revealing enzyme interactions, quinary structure, and domain motion in glycolytic enzymes.

DOI 10.1101/2022.09.13.507800

humanstructural biology

𝕏 PostBluesky

BiophysicsBiophysical JournalPeer-reviewedMar 1, 2020

The interplay between molten globules and heme disassociation defines human hemoglobin disassembly

P. P. Samuel, M. A. White, W. C. Ou…·J. S. Olson

This paper develops a quantitative model of human hemoglobin disassembly, showing that heme dissociation and molten globule intermediates drive structural changes, leading to pathophysiological outcomes like Heinz bodies and hemolysis.

DOI 10.1016/j.bpj.2020.01.031

humanproteomics

𝕏 PostBluesky