Author

L. E. Kay

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· 5 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:protein folding & dynamics· 3 Assay:structural biology· 3 Organism:bacteria (other)· 2 Approach:biophysical modeling· 2 Assay:cryo-EM· 2 Research Focus:cell type annotation· 1 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

Z. A. Ripstein· 4 shared J. L. Rubinstein· 3 shared E. Rennella· 2 shared S. Vahidi· 2 shared A. K. Mittermaier· 1 shared A. L. Goldberg· 1 shared C. R. Knoverek· 1 shared G. R. Bowman· 1 shared

Activity by Year

2017-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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4 shared papersBiophysics

Z. A. Ripstein

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Author profile →

6 papers

Recent·Most cited

Flexible client-dependent cages in the assembly landscape of the periplasmic protease-chaperone DegP

R. W. Harkness, Z. A. Ripstein, J. M. Di Trani, L. E. Kay

The paper investigates how DegP forms flexible cage structures in response to different client sizes, revealing their structural diversity and functional roles in protein homeostasis.

bioRxiv · Oct 17, 2022Biophysics

Opening of a Cryptic Pocket in β-lactamase Increases Penicillinase Activity

C. R. Knoverek, U. L. Mallimadugula, S. Singh, E. Rennella, T. E. Frederick, T. Yuwen, S. Raavicharla, L. E. Kay, G. R. Bowman

The paper investigates how a cryptic pocket in β-lactamase, formed under the Ω-loop, enhances enzyme activity against penicillin, suggesting excited states can improve function.

bioRxiv · Apr 14, 2021Biophysics

An allosteric switch regulates Mycobacterium tuberculosis ClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR

S. Vahidi, Z. A. Ripstein, J. B. Juravsky, E. Rennella, A. L. Goldberg, A. K. Mittermaier, J. L. Rubinstein, L. E. Kay

This paper identifies an allosteric switch in Mycobacterium tuberculosis ClpP1P2 protease that regulates its activity through conformational changes, revealed by cryo-EM and methyl-TROSY NMR.

Proceedings of the National Academy of Sciences · Mar 2, 2020Peer-reviewedBiophysics

A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery

Z. A. Ripstein, S. Vahidi, W. A. Houry, J. L. Rubinstein, L. E. Kay

This study presents cryo-EM structures of the ClpXP complex from Neisseria meningitidis, revealing how ATP hydrolysis couples substrate unfolding and proteolysis.

bioRxiv · Dec 8, 2019Biophysics

Atomic Resolution Mechanism of Ligand Binding to a Solvent Inaccessible Cavity in T4 Lysozyme

J. Mondal, N. Ahalawat, S. Pandit, L. E. Kay, P. Vallurupalli

This study uses molecular dynamics simulations to reveal the atomistic mechanism of benzene binding to a solvent-inaccessible cavity in L99A T4L, showing that subtle helix movements enable rapid ligand access without large conformational changes.

bioRxiv · Feb 4, 2018Biophysics

Structure of a AAA+ unfoldase in the process of unfolding substrate

Z. A. Ripstein, R. Huang, R. Augustyniak, L. E. Kay, J. L. Rubinstein

The paper captures the structure of VAT, an AAA+ unfoldase, during substrate unfolding using cryo-EM, revealing a hand-over-hand mechanism.

bioRxiv · Feb 4, 2017Biochemistry