Author

Y. Joti

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· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Assay:protein structure· 2 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1 Approach:statistical model· 1 Assay:structural biology· 1 Research Focus:synaptic & neural circuits· 1

Frequent Co-Authors

E. Nango· 2 shared K. Tono· 2 shared R. Tanaka· 2 shared S. Iwata· 2 shared A. D. Diethelm· 1 shared A. Furrer· 1 shared A. Kitao· 1 shared A. Wach· 1 shared

Activity by Year

2017-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 32 mutual co-author links

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2 shared papersBiochemistry

E. Nango

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

ULTRAFAST STRUCTURAL CHANGES DIRECT THE FIRST MOLECULAR EVENTS OF VISION

T. Gruhl, T. Weinert, M. Rodrigues, C. J. Milne, G. Ortolani, K. Nass, E. Nango, S. Sen, P. J. Johnson, C. Cirelli, A. Furrer, S. Mous, P. Skopintsev, D. James, F. Dworkowski, , Scher

This study uses ultrafast crystallography to reveal how photoactivated retinal initiates structural changes in rhodopsin, leading to GPCR activation and vision.

bioRxiv · Oct 14, 2022 · PreprintBiochemistry

An efficient timer and sizer of biomacromolecular motions

J. Chan, H.-R. Lin, K. Takemura, K.-C. Chang, Y.-Y. Chang, Y. Joti, A. Kitao, L.-W. Yang

The paper develops an efficient method to estimate the time scales and sizes of slow protein motions using elastic network models and power laws validated by NMR data.

bioRxiv · Apr 11, 2019Biophysics

Atomic resolution structure of serine protease proteinase K at ambient temperature

T. Masuda, M. Suzuki, S. Inoue, C. Song, T. Nakane, E. Nango, R. Tanaka, K. Tono, Y. Joti, T. Kameshima, T. Hatsui, M. Yabashi, B. Mikami, O. Nureki, K. Numata, , M. Sugahara

The paper reports an atomic resolution structure of proteinase K at ambient temperature using serial femtosecond crystallography, revealing hydrogen atoms, water molecules, and side-chain conformations.

bioRxiv · Feb 21, 2017Biochemistry