Author

N. C. Jones

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· 4 Biochemistry· 2 Animal Behavior & Cognition· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Research Focus:protein folding & dynamics· 3 Assay:protein structure· 3 Research Focus:benchmarking· 2 Research Focus:cell signaling & trafficking· 2 Approach:deep learning· 2 Organism:human· 2 Research Focus:protein structure prediction· 2

Frequent Co-Authors

S. V. Hoffmann· 7 shared P. Kursula· 3 shared A. Raasakka· 2 shared G. Nagy· 2 shared S. Ruskamo· 2 shared A. Sutinen· 1 shared A. Zipori· 1 shared C. K. Kristiansen· 1 shared

Activity by Year

2019-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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7 shared papersBiophysics

S. V. Hoffmann

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

A Reference Data Set for Circular Dichroism Spectroscopy Comprised of Validated Intrinsically Disordered Protein Models

G. Nagy, N. C. Jones, S. V. Hoffmann, H. Grubmueller

The paper provides a reference dataset of validated intrinsically disordered protein models and their CD spectra to assess the accuracy of CD prediction tools.

bioRxiv · Oct 19, 2023Biophysics

Conformational analysis of membrane-proximal segments of GDAP1 in a lipidic environment using synchrotron radiation suggests a mode of assembly at the mitochondrial outer membrane

A. Sutinen, N. C. Jones, S. V. Hoffmann, S. Ruskamo, P. Kursula

This study uses synchrotron radiation and spectroscopy to model GDAP1 assembly at the mitochondrial outer membrane, suggesting a single transmembrane helix flanked by peripheral helices.

bioRxiv · May 8, 2023Biochemistry

Mouse behaviour on the trial-unique non-matching-to-location (TUNL) touchscreen task reflects a mixture of distinct working memory codes and response biases

D. Bennett, J. Nakamura, C. Vinnakota, E. Sokolenko, J. Nithianantharajah, M. van den Buuse, N. C. Jones, S. Sundram, R. Hill

This study uses computational modeling to show that mouse behavior on the TUNL task reflects a mix of spatial and prospective working memory along with response biases, challenging the assumption that it solely measures spatial working memory.

bioRxiv · Oct 30, 2022Animal Behavior & Cognition

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

Helix formation during the coupled binding and folding of intrinsically disordered proteins monitored by synchrotron-radiation circular dichroism spectroscopy

E. Karlsson, E. Andersson, N. C. Jones, S. V. Hoffmann, P. Jemth, M. Kjaergaard

The paper uses synchrotron-radiation circular dichroism to study helix formation during the binding of intrinsically disordered proteins, revealing kinetic phases and structural intermediates.

bioRxiv · May 16, 2019Biophysics

SESCA: Predicting Circular Dichroism Spectra from Protein Molecular Structures

G. Nagy, M. Igaev, S. V. Hoffmann, N. C. Jones, H. Grubmuller

SESCA predicts circular dichroism spectra from protein structures, outperforming existing methods with 50% smaller average deviation.

bioRxiv · Feb 25, 2019Biophysics

Neuropathy-related mutations alter the membrane binding properties of the human myelin protein P0 cytoplasmic tail

A. Raasakka, S. Ruskamo, R. Barker, O. C. Krokengen, G. H. Vatne, C. K. Kristiansen, E. I. Hallin, M. W. Skoda, U. Bergmann, H. Wacklin-Knecht, N. C. Jones, S. V. Hoffmann, P. Kursula

This study investigates how neuropathy-related mutations in the cytoplasmic tail of the human myelin protein P0 affect its membrane binding properties and function.

bioRxiv · Jan 30, 2019Biophysics

Ionic strength and calcium regulate the membrane interactions of myelin basic protein and the cytoplasmic domain of myelin protein zero

A. Raasakka, N. C. Jones, S. V. Hoffmann, P. Kursula

This study investigates how ionic strength and calcium influence the membrane interactions of myelin basic protein and the cytoplasmic domain of P0, showing their impact on lipid vesicle aggregation.

bioRxiv · Jan 24, 2019Biochemistry