Author

M. H. Seaberg

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· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 2 Assay:structural biology· 2 Research Focus:drug response / drug discovery· 1 Assay:protein structure· 1 Approach:statistical model· 1 Organism:virus· 1

Frequent Co-Authors

M. S. Hunter· 3 shared R. G. Sierra· 3 shared A. Barty· 2 shared A. Batyuk· 2 shared A. Tolstikova· 2 shared B. Hayes· 2 shared B. Yuksel· 2 shared C. Dag· 2 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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3 shared papersBiophysics

M. S. Hunter

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3 papers

Recent·Most cited

Detection of a geminate photoproduct of bovine cytochrome c oxidase by time-resolved serial femtosecond crystallography

S.-R. Yeh, I. Ishigami, D. L. Rousseau, S. Carbajo, N. Zatsepin, J. Coe, M. Hikita, M. H. Seaberg, R. G. Sierra, M. S. Hunter, P. Fromme, R. Fromme, G. Nelson, T. Grant, S. Basu, C. Conrad

The paper detects a geminate photoproduct of bovine cytochrome c oxidase using time-resolved serial femtosecond crystallography, revealing the ligand dissociation trajectory and protein dynamics.

bioRxiv · May 8, 2023Biophysics

Cooperative Allostery and Structural Dynamics of Streptavidin at Cryogenic- and Ambient-temperature

E. Ayan, B. Yuksel, E. Destan, F. B. Ertem, G. Yildirim, M. Eren, O. M. Yefanov, A. Barty, A. Tolstikova, G. K. Ketawala, S. Botha, E. H. Dao, B. Hayes, M. Liang, M. H. Seaberg, , H. DeMirci

The paper presents two apo-streptavidin structures at different temperatures and reveals cooperative allostery through water-mediated interactions.

bioRxiv · Sep 23, 2021Biophysics

Near-Physiological-Temperature Serial Femtosecond X-ray Crystallography Reveals Novel Conformations of SARS-CoV-2 Main Protease Active Site for Improved Drug Repurposing

S. Durdagi, C. Dag, B. Dogan, M. Yigin, T. Avsar, C. Buyukdag, I. Erol, F. B. Ertem, S. Calis, G. Yildirim, M. Orhan, O. Guven, B. Aksoydan, E. Destan, K. Sahin, , Sn

The paper determines two apo structures of SARS-CoV-2 main protease at near-physiological temperature using SFX and uses molecular simulations to analyze inhibitor binding for drug repurposing.

bioRxiv · Sep 9, 2020Biophysics