M
Matthew M. Copeland
Researcher at University of Kansas
Publications - 10
Citations - 87
Matthew M. Copeland is an academic researcher from University of Kansas. The author has contributed to research in topics: Medicine & Computer science. The author has an hindex of 1, co-authored 2 publications receiving 41 citations.
Papers
More filters
Journal ArticleDOI
Dockground: A comprehensive data resource for modeling of protein complexes
Petras J. Kundrotas,Ivan Anishchenko,Taras Dauzhenka,Ian Kotthoff,Daniil Mnevets,Matthew M. Copeland,Ilya A. Vakser +6 more
TL;DR: A comprehensive description of the Dockground resource is presented, including previously unpublished unbound docking benchmark set 4, and the X‐ray docking decoy set 2, for structural modeling of protein interactions.
Book ChapterDOI
Dockground Tool for Development and Benchmarking of Protein Docking Procedures.
TL;DR: A description and a guide to the DOCKGROUND resource ( http://dockground.ku.edu ) for structural modeling of protein interactions is presented, which integrates various datasets of protein complexes and other data for the development and testing of protein docking techniques.
Journal ArticleDOI
Gaussian Accelerated Molecular Dynamics in OpenMM.
Matthew M. Copeland,Hung N. Do,Lane W. Votapka,Keya Joshi,Jian Wang,Rommie E. Amaro,Yinglong Miao +6 more
TL;DR: The implementation of GaMD in the OpenMM simulation package is presented and it is validated on model systems of alanine dipeptide and RNA folding to allow for wider applications in simulations of proteins, RNA, and other biomolecules.
Journal ArticleDOI
GWYRE: A Resource for Mapping Variants onto Experimental and Modeled Structures of Human Protein Complexes
Sukhaswami Malladi,Harold R. Powell,Alessia David,Suhail A. Islam,Matthew M. Copeland,Petras J. Kundrotas,Michael J.E. Sternberg,Ilya A. Vakser +7 more
TL;DR: The GWYRE (Genome Wide PhYRE) project as discussed by the authors uses knowledge-based tertiary structure prediction and quaternary structure prediction using template-based docking by a full-structure alignment protocol.
Journal ArticleDOI
MAHOMES II: A webserver for predicting if a metal binding site is enzymatic
TL;DR: In this article , the physicochemical features were used to distinguish between metalloenzyme and non-enzyme sites, and an improved classifier was proposed to identify protein bound metal sites as enzymatic or non-enzymatic with 94% precision and 92% recall.