Author

M. Morais

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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Research Focus:protein folding & dynamics· 4 Approach:experimental assay· 3 Assay:structural biology· 3 Organism:bacteria (other)· 2 Approach:biophysical modeling· 2 Research Focus:chromatin & epigenetic regulation· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

B. A. Kelch· 1 shared B. J. Hilbert· 1 shared B. P. Mahler· 1 shared C. Bussetta· 1 shared C. E. Catalano· 1 shared C. R. Davis· 1 shared E. A. Dill· 1 shared E. Dill· 1 shared

Activity by Year

2020-2022 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 8 mutual co-author links

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1 shared paperBiophysics

B. A. Kelch

Mutual co-authors in cluster

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4 papers

Recent·Most cited

Biophysical and Structural Characterization of a Viral Genome Packaging Motor

N. S. Prokhorov, C. R. Davis, K. Maruthi, Q. Yang, M. Woodson, M. A. White, L. M. Miller, M. F. Jarrold, C. E. Catalano, M. Morais

This paper characterizes the biophysical properties and initial structure of λ terminase during DNA translocation, showing a pentameric complex with flexibility and ATP hydrolysis activity.

bioRxiv · Sep 25, 2022 · PreprintBiophysics

Viral Packaging ATPases Utilize a Glutamate Switch to Couple ATPase Activity and DNA Translocation

J. Pajak, R. Atz, B. J. Hilbert, M. Morais, B. A. Kelch, P. Jardine, G. Arya

This study identifies a glutamate switch mechanism in viral packaging ATPases that couples ATP binding to DNA translocation through conformational changes.

bioRxiv · Dec 1, 2020Biophysics

The NMR structure of a vestigial nuclease provides insight into the evolution of functional transitions in viral dsDNA packaging motors

B. P. Mahler, P. J. Bujalowski, H. Mao, E. A. Dill, P. J. Jardine, K. H. Choi, M. Morais

The paper reports the NMR structure of a vestigial nuclease domain in phi29 ATPase, revealing its evolutionary origin and role in DNA packaging motor function.

Nucleic Acids Research · Nov 18, 2020Peer-reviewedBiophysics

Biochemical and Biophysical Characterization of the dsDNA packaging motor from the Lactococcus lactis bacteriophage asccphi28

E. Reyes-Aldrete, E. Dill, C. Bussetta, M. R. Szymanski, G. S. Diemer, P. Maindola, M. White, K. Choi, M. Morais

The paper characterizes the ATPase motor of Lactococcus lactis phage asccphi28, showing it forms functional rings in solution and has ATPase activity comparable to capsid-bound motors.

bioRxiv · Nov 17, 2020Biophysics