Author

H. T. Kratochvil

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· 2 Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein structure prediction· 2 Organism:virus· 2 Assay:cryo-EM· 1 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1 Approach:mechanistic / dynamical model· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

G. E. Merz· 3 shared A. F. Brilot· 2 shared A. M. Smith· 2 shared A. N. Rizo· 2 shared C. M. Azumaya· 2 shared D. Diwanji· 2 shared F. Li· 2 shared H. C. Nguyen· 2 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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3 shared papersBiochemistry

G. E. Merz

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Transient Water Wires Mediate Selective Proton Conduction in Designed Channel Proteins

H. T. Kratochvil, L. C. Watkins, M. Mravic, N. H. Somberg, J. L. Thomaston, J. M. Nicoludis, L. Liu, M. Hong, G. A. Voth, W. DeGrado

The paper designs proton-conducting channels that use transient water wires to achieve high selectivity for protons over sodium ions.

bioRxiv · Mar 28, 2022Biophysics

CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes.

M. Gupta, C. M. Azumaya, M. Moritz, S. Pourmal, A. Diallo, G. E. Merz, G. M. Jang, M. Bouhaddou, A. Fossati, A. F. Brilot, D. Diwanji, E. Hernandez, N. Herrera, H. T. Kratochvil, V. L. Lam, , K. I Pawar

The paper uses cryo-EM and AlphaFold2 to determine the structure of SARS-CoV-2 Nsp2, revealing its zinc-binding site and potential interactions with host proteins.

bioRxiv · May 10, 2021 · PreprintBiophysics

Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking

M. Schuller, G. J. Correy, S. Gahbauer, D. Fearon, T. Wu, R. E. Diaz, I. D. Young, L. Carvalho Martins, D. H. Smith, U. Schulze-Gahmen, T. W. Owens, I. Deshpande, G. E. Merz, A. C. Thwin, J. T. Biel, , Smi

The paper identifies new chemical fragments binding to the SARS-CoV-2 Nsp3 macrodomain through crystallographic screening and computational docking, validating their binding with biophysical techniques.

bioRxiv · Nov 24, 2020Biochemistry

An ultra-potent synthetic nanobody neutralizes SARS-CoV-2 by locking Spike into an inactive conformation

M. Schoof, B. Faust, R. A. Saunders, S. Sangwan, V. V. Rezelj, N. Hoppe, M. Boone, C. Billesboelle, C. Puchades, C. M. Azumaya, H. T. Kratochvil, M. Zimanyi, I. Deshpande, J. Liang, S. Dickinson, , Barile-H

This paper develops a potent synthetic nanobody that neutralizes SARS-CoV-2 by locking its Spike protein in an inactive conformation, enabling aerosol delivery as a prophylactic or therapeutic agent.

bioRxiv · Aug 8, 2020Biochemistry