Author

J. M. Aramini

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

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 3 Assay:protein structure· 2 Approach:mechanistic / dynamical model· 1 Approach:microscopy & imaging analysis· 1 Organism:plant (other)· 1 Assay:protein sequence· 1 Assay:proteomics· 1

Frequent Co-Authors

K. H. Gardner· 3 shared D. Gagne· 2 shared U. R. Edupuganti· 2 shared X. Xu· 2 shared A. A. Gil· 1 shared A. Lukacs· 1 shared B. A. Johnson· 1 shared C. L. Simmerling· 1 shared

Activity by Year

2020-2021 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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3 shared papersBiophysics

K. H. Gardner

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Author profile →

4 papers

Recent·Most cited

Dynamics in Natural and Designed Elastins and Their Relation to Elastic Fiber Structure and Recoil

M. F. C. A. Carvajal, J. M. Preston, N. M. Jamhawi, T. M. Sabo, S. Bhattacharya, J. M. Aramini, R. J. Wittebort, R. Koder

This study uses NMR to analyze the dynamics of elastin mimetics and fibers, finding high disorder and suggesting hydrophobic effects drive elastic recoil rather than entropy loss.

Biophysical Journal · Oct 1, 2021Peer-reviewedBiophysics

Use of High Pressure NMR Spectroscopy to Rapidly Identify Proteins with Internal Ligand-Binding Voids

D. Gagne, R. Azad, J. M. Aramini, X. Xu, E. A. Isiorho, U. R. Edupuganti, J. P. Williams, L. P. Marcelino, B. A. Johnson, K. Akasaka, K. H. Gardner

This paper introduces a method using high-pressure NMR spectroscopy to identify proteins with internal ligand-binding voids by detecting nonlinear chemical shift changes in 1H/15N HSQC experiments.

bioRxiv · Aug 25, 2020 · PreprintBiophysics

High-Pressure NMR Reveals Volume and Compressibility Differences Between Two Stably Folded Protein Conformations

X. Xu, D. Gagne, J. M. Aramini, K. H. Gardner

The paper uses high-pressure NMR to study conformational changes in ARNT PAS-B Y456T, finding that the slipped conformation is smaller and less compressible than the wildtype and involves an unfolded intermediate.

bioRxiv · Jul 29, 2020Biophysics

Unraveling the Mechanism of a LOV Domain Optogenetic Sensor: A Glutamine Lever Induces Unfolding of the Jα Helix

J. N. Iuliano, J. Tolentino Collado, A. A. Gil, P. V. Ravindran, A. Lukacs, S. Shin, H. A. Woroniecka, K. Adamczyk, J. M. Aramini, U. R. Edupuganti, C. R. Hall, G. M. Greetham, I. V. Sazanovich, I. P. Clark, T. Daryaee, , P. J. Tonge

This study investigates the structural dynamics of the LOV2 domain in AsLOV2, showing that Q513 and N414 mediate J-helix unfolding linked to optogenetic function.

bioRxiv · Jan 29, 2020Biophysics