G
Guillermo A. Bermejo
Researcher at Center for Information Technology
Publications - 11
Citations - 395
Guillermo A. Bermejo is an academic researcher from Center for Information Technology. The author has contributed to research in topics: Residual dipolar coupling & Glutamine binding. The author has an hindex of 7, co-authored 11 publications receiving 298 citations.
Papers
More filters
Journal ArticleDOI
Xplor-NIH for molecular structure determination from NMR and other data sources
TL;DR: Xplor‐NIH is a popular software package for biomolecular structure determination from nuclear magnetic resonance (NMR) and other data sources, and some of its most useful data‐associated energy terms are reviewed.
Journal ArticleDOI
Smooth statistical torsion angle potential derived from a large conformational database via adaptive kernel density estimation improves the quality of NMR protein structures
TL;DR: A new statistical torsion angle potential is developed using adaptive kernel density estimation to extract probability densities from a large database of more than 106 quality‐filtered amino acid residues, and results in protein structures with improved conformation, nonbonded atomic interactions, and accuracy.
Journal ArticleDOI
Structural mechanism of Bax inhibition by cytomegalovirus protein vMIA
TL;DR: The structure suggests that by stabilizing key elements in Bax needed to unravel for its MOM insertion and oligomerization, vMIA prevents these important steps in apoptosis.
Journal ArticleDOI
Improving NMR Structures of RNA
TL;DR: RNA-ff1, a new force field for structure calculation with Xplor-NIH, improves covalent geometry and MolProbity validation criteria for clashes and backbone conformation in most cases and shows great promise in bridging the quality gap that separates NMR and X-ray structures of RNA.
Journal ArticleDOI
Accurate High-Throughput Structure Mapping and Prediction with Transition Metal Ion FRET
TL;DR: It is reported that transition metal ion FRET (tmFRET) can be used in a rapid, highly parallel screen, to determine distances from multiple locations within a protein at extremely low concentrations, which opens the door to rapid, accurate mapping and prediction of protein structures atLow concentrations, in large complex systems, and in living cells.