Author

M. B. A. Kunze

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biophysics· 3

Signature Assays, Organisms & Methods

Click to filter · or open tag

Assay:protein structure· 3 Approach:deep learning· 2 Research Focus:software / tool· 2 Research Focus:chromatin & epigenetic regulation· 1 Approach:experimental assay· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Approach:statistical model· 1

Frequent Co-Authors

K. Lindorff-Larsen· 3 shared G. Tesei· 2 shared J. M. Martins· 2 shared R. Crehuet· 2 shared A. Escobedo· 1 shared B. Eftekharzadeh· 1 shared B. Topal· 1 shared D. Montepietra· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersBiophysics

K. Lindorff-Larsen

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

BiophysicsbioRxivPreprintJan 27, 2023

FRETpredict: A Python package for FRET efficiency predictions using rotamer libraries

D. Montepietra, G. Tesei, J. M. Martins…·K. Lindorff-Larsen

FRETpredict predicts FRET efficiencies from protein conformations using rotamer libraries, validated on various systems and available as open-source software.

DOI 10.1101/2023.01.27.525885

protein structuredeep learning

𝕏 PostBluesky

BiophysicsbioRxivAug 9, 2020

DEER-PREdict: Software for Efficient Calculation of Spin-Labeling EPR and NMR Data from Conformational Ensembles

G. Tesei, J. M. Martins, M. B. A. Kunze…·K. Lindorff-Larsen

DEER-PREdict calculates EPR and NMR data from protein conformational ensembles to validate models and interpret experiments.

DOI 10.1371/journal.pcbi.1008551

protein structuredeep learning

𝕏 PostBluesky

BiophysicsbioRxivFeb 28, 2019

Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in the activation domain of a transcription factor

A. Escobedo, B. Topal, M. B. A. Kunze…·X. Salvatella

This study investigates how polyglutamine tract length affects the structure and function of the androgen receptor, revealing hydrogen bonds that stabilize a helical conformation linked to transcriptional activity and disease.

DOI 10.1038/s41467-019-09923-2

humanprotein structure

𝕏 PostBluesky