Author

T. Löhr

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:deep learning· 2 Research Focus:protein folding & dynamics· 2 Approach:statistical model· 2 Assay:cryo-EM· 1 Approach:experimental assay· 1 Assay:long-read sequencing· 1 Research Focus:protein structure prediction· 1 Assay:structural biology· 1

Frequent Co-Authors

M. Vendruscolo· 3 shared C. Camilloni· 2 shared G. T. Heller· 2 shared K. Kohlhoff· 2 shared M. Bonomi· 1 shared S. E. Hoff· 1 shared S. Truong· 1 shared Z. F. Brotzakis· 1 shared

Activity by Year

2020-2022 · peak 1/yr

Co-Author Collaboration Network

8 top collaborators · 16 mutual co-author links

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3 shared papersBiophysics

M. Vendruscolo

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Author profile →

3 papers

Recent·Most cited

BiophysicsbioRxivMay 29, 2022

Determination of the structure and dynamics of the fuzzy coat of an amyloid fibril of IAPP using cryo-electron microscopy

Z. F. Brotzakis, T. Löhr, S. Truong…·M. Vendruscolo

The paper develops MEMMI, a cryo-EM method that determines structure and dynamics of large systems, and applies it to study the fuzzy coat of an IAPP amyloid fibril.

DOI 10.1021/acs.biochem.3c00010

cryo-EMdeep learning

𝕏 PostBluesky

BiophysicsbioRxivPreprintNov 10, 2021

A small molecule stabilises the disordered native state of the Alzheimer's Aβ peptide

T. Löhr, K. Kohlhoff, G. T. Heller…·M. Vendruscolo

This study identifies a small molecule that stabilizes the disordered native state of the Alzheimer's Aβ42 peptide through dynamic binding involving π-stacking and entropic effects.

DOI 10.1101/2021.11.10.468059

experimental assayprotein folding & dynamics

𝕏 PostBluesky

BiophysicsbioRxivMay 7, 2020

A kinetic ensemble of the Alzheimer's Aβ peptide

T. Löhr, K. Kohlhoff, G. T. Heller…·M. Vendruscolo

This study develops a Markov state model to determine the kinetic ensemble of Aβ42, revealing fast inter-state transitions and predominantly unfolded or short-lived partially-folded states.

DOI 10.1038/s43588-020-00003-w

long-read sequencingstructural biology

𝕏 PostBluesky