Author

C. L. Hoop

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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Research Focus:protein folding & dynamics· 3 Assay:protein structure· 2 Approach:experimental assay· 1 Organism:human· 1 Approach:mechanistic / dynamical model· 1 Approach:statistical model· 1 Assay:structural biology· 1

Frequent Co-Authors

J. Baum· 3 shared B. Wang· 2 shared J. K. Williams· 2 shared A. Sam· 1 shared C. A. Tobita· 1 shared D. A. Case· 1 shared J. Zhu· 1 shared S. Bhattacharya· 1 shared

Activity by Year

2019-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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3 shared papersBiophysics

J. Baum

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3 papers

Recent·Most cited

Molecular Dynamics Analysis of a Flexible Loop at the Binding Interface of the SARS-CoV-2 Spike Protein Receptor-Binding Domain

J. K. Williams, B. Wang, A. Sam, C. L. Hoop, D. A. Case, J. Baum

This paper uses molecular dynamics simulations to analyze the conformational flexibility of the SARS-CoV-2 RBD Loop 3 and identifies new unbound substates that could be therapeutic targets.

bioRxiv · Jan 8, 2021Biophysics

NMR unveils an N-terminal interaction interface on acetylated-α-synuclein monomers for recruitment to fibrils

X. Yang, B. Wang, C. L. Hoop, J. K. Williams, J. Baum

This paper identifies an N-terminal binding interface on acetylated-α-synuclein monomers that interacts with fibrils and off-pathway oligomers, revealing a mechanism for fibril elongation and potential therapeutic targets.

bioRxiv · Aug 17, 2020Biophysics

Collagen I weakly interacts with the β-sheets of β2-microglobulin and enhances conformational exchange to induce amyloid formation

C. L. Hoop, J. Zhu, S. Bhattacharya, C. A. Tobita, S. E. Radford, J. Baum

This study shows collagen I weakly interacts with β2-microglobulin, promoting conformational exchange that leads to amyloid formation.

bioRxiv · Oct 11, 2019Biophysics