Author

H. J. Lessen

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· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Approach:mechanistic / dynamical model· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Approach:statistical model· 1

Frequent Co-Authors

K. G. Fleming· 2 shared A. H. Beaven· 1 shared A. J. Sodt· 1 shared A. J. Wand· 1 shared A. M. Faustino· 1 shared A. M. Plummer· 1 shared B. Fuglestad· 1 shared B. S. Marques· 1 shared

Activity by Year

2019-2022 · peak 1/yr

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10 top collaborators · 17 mutual co-author links

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2 shared papersBiophysics

K. G. Fleming

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3 papers

Recent·Most cited

Molecular mechanisms of spontaneous curvature and softening in complex lipid bilayer mixtures

H. J. Lessen, K. C. Sapp, A. H. Beaven, R. Ashkar, A. J. Sodt

This study uses molecular dynamics simulations to test assumptions about lipid curvature and bilayer mechanics, finding non-additive curvature preferences and two mechanisms of bilayer softening.

bioRxiv · Feb 17, 2022Biophysics

Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy

E. S. O'Brien, B. Fuglestad, H. J. Lessen, M. A. Stetz, D. W. Lin, B. S. Marques, K. Gupta, K. G. Fleming, A. J. Wand

This study characterizes the fast internal motion and residual conformational entropy of membrane proteins using solution NMR relaxation techniques, revealing unique dynamics compared to soluble proteins.

bioRxiv · Apr 2, 2020Biophysics

SurA is a "Groove-y" Chaperone That Expands Unfolded Outer Membrane Proteins

D. C. Marx, A. M. Plummer, A. M. Faustino, M. A. Roskopf, M. J. Leblanc, T. Devlin, H. J. Lessen, B. T. Amann, P. J. Fleming, S. Krueger, S. D. Fried, K. G. Fleming

This paper investigates how SurA, a bacterial chaperone, interacts with unfolded outer membrane proteins (uOMPs) using structural biology techniques, revealing distinct binding modes and a mechanism for uOMP expansion.

bioRxiv · Dec 17, 2019Biophysics