Author

H. M. Dokainish

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 Microbiology· 1

Signature Assays, Organisms & Methods

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Organism:virus· 3 Approach:mechanistic / dynamical model· 2 Research Focus:protein folding & dynamics· 2 Assay:structural biology· 2 Assay:cryo-EM· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

Y. Sugita· 2 shared A. Takasu· 1 shared C. Kobayashi· 1 shared D. I. Stuart· 1 shared H. Fukuhara· 1 shared H. Sawa· 1 shared J. Jung· 1 shared J. T. Huiskonen· 1 shared

Activity by Year

2021-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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2 shared papersBiophysics

Y. Sugita

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Native spike flexibility revealed by BSL3 Cryo-ET of active SARS-CoV-2 virions

H. Fukuhara, H. M. Dokainish, S. Kita, K. Tabata, A. Takasu, J. T. Huiskonen, Y. Anraku, T. Nomai, T. Someya, T. Senda, D. I. Stuart, M. Sasaki, Y. Orba, Y. Suzuki, H. Sawa, K. Maenaka

This study uses cryo-ET to analyze native, active SARS-CoV-2 virions, revealing a transient open-trimer prefusion state and hidden spike flexibility with implications for vaccine design.

bioRxiv · Oct 10, 2023 · PreprintMicrobiology

Structural Ramifications of Spike Protein D614G Mutation in SARS-CoV-2

H. M. Dokainish, Y. Sugita

This study investigates the structural impact of the D614G mutation in SARS-CoV-2 Spike protein using molecular dynamics simulations, revealing its role in enhancing infectivity and stabilizing the protein structure.

bioRxiv · Jan 24, 2022 · PreprintBiophysics

The Inherent Flexibility of Receptor Binding Domains in SARS-CoV-2 Spike Protein

H. M. Dokainish, S. Re, T. Mori, C. Kobayashi, J. Jung, Y. Sugita

This study identifies multiple conformational states of the SARS-CoV-2 Spike protein's receptor binding domain through molecular dynamics simulations, highlighting structural flexibility important for drug and vaccine design.

bioRxiv · Aug 6, 2021Biophysics