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Willy Wriggers

Researcher at University of Texas Health Science Center at Houston

Publications -  44
Citations -  4053

Willy Wriggers is an academic researcher from University of Texas Health Science Center at Houston. The author has contributed to research in topics: Actin & Protein structure. The author has an hindex of 29, co-authored 40 publications receiving 3911 citations. Previous affiliations of Willy Wriggers include University of California, San Diego & Scripps Research Institute.

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Situs: A package for docking crystal structures into low-resolution maps from electron microscopy.

TL;DR: A set of visualization and analysis procedures, termed the Situs package, has been developed to provide an efficient and robust method for the localization of protein subunits in low-resolution data.
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Multi-resolution contour-based fitting of macromolecular structures

TL;DR: A novel contour-based matching criterion is presented for the quantitative docking of high-resolution structures of components into low-resolution maps of macromolecular complexes and enables for the first time the reliable docking of smaller molecular components into EM densities of large biomolecular assemblies at such low resolutions.
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Like-charge attraction between polyelectrolytes induced by counterion charge density waves

TL;DR: This work directly observed the organization of multivalent ions on cytoskeletal filamentous actin by using synchrotron x-ray diffraction and discovered an unanticipated symmetry-breaking collective counterion mechanism for generating attractions, which can fundamentally impinge on general understanding of electrostatics in aqueous media.
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Actin Depolymerizing Factor Stabilizes an Existing State of F-Actin and Can Change the Tilt of F-Actin Subunits

TL;DR: Although ADF changes the mean twist of actin, it is shown that it does this by stabilizing a preexisting F-actin angular conformation by binding to a site on the opposite side of F-Actin from that of the previously described ADF binding site.
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Using situs for flexible and rigid-body fitting of multiresolution single-molecule data.

TL;DR: Test calculations on isoforms of actin and lactoferrin demonstrate that the flexible docking faithfully reproduces conformational differences with a precision < 2 A if atomic structures are locally conserved.