Author

T. Santl-Temkiv

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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Microbiology· 2 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:bacteria (other)· 2 Approach:deep learning· 1 Research Focus:host-pathogen & immune response· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

K. W. Finster· 2 shared T. Boesen· 2 shared T. Drace· 2 shared A. Zipori· 1 shared C. Melvad· 1 shared C. Wieber· 1 shared D. Niedermeier· 1 shared G. Kramer· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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2 shared papersMicrobiology

K. W. Finster

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Author profile →

3 papers

Recent·Most cited

Micro-PINGUIN: Microtiter plate-based ice nucleation detection in gallium with an infra-red camera

C. Wieber, M. R. Jeppesen, K. W. Finster, C. Melvad, T. Santl-Temkiv

The paper introduces a new droplet freezing instrument, micro-PINGUIN, for measuring ice nucleation particles and demonstrates its accuracy and reproducibility.

bioRxiv · Sep 27, 2023Microbiology

Structure and Protein-Protein Interactions of Ice Nucleation Proteins Drive Their Activity

S. Hartmann, M. Ling, L. S. A. Dreyer, A. Zipori, K. W. Finster, S. Grawe, L. Z. Jensen, S. Borck, N. Reicher, T. Drace, D. Niedermeier, N. C. Jones, S. V. Hoffmann, H. Wex, Y. Rudich, , T. Santl-Temkiv

The paper determines the structure and protein-protein interactions of ice nucleation proteins and shows they are essential for their activity.

bioRxiv · Jan 21, 2022Microbiology

The Ice Nucleating Protein InaZ is Activated by Low Temperature

S. J. Roeters, T. W. Golbek, M. Bregnhoj, T. Drace, S. Alamdari, W. Roseboom, G. Kramer, T. Santl-Temkiv, K. Finster, S. Woutersen, J. Pfaendtner, T. Boesen, T. Weidner

This study investigates how the ice-nucleating protein InaZ from Pseudomonas syringae folds and interacts with water at low temperatures, revealing structural changes that enhance ice nucleation.

bioRxiv · May 15, 2020 · PreprintBiophysics