about
The structural and biochemical characterizations of a novel TET peptidase complex from Pyrococcus horikoshii reveal an integrated peptide degradation system in hyperthermophilic ArchaeaStructure of the K-turn U4 RNA: a combined NMR and SANS studyThe structure of the box C/D enzyme reveals regulation of RNA methylationStructural basis for the assembly of the Sxl-Unr translation regulatory complexProbing the conformation of FhaC with small-angle neutron scattering and molecular modeling.Effects of hydrostatic pressure on the quaternary structure and enzymatic activity of a large peptidase complex from Pyrococcus horikoshii.Uniqueness of models from small-angle scattering data: the impact of a hydration shell and complementary NMR restraints.Amphipols from A to Z.Sequence-specific mapping of the interaction between urea and unfolded ubiquitin from ensemble analysis of NMR and small angle scattering data.Conformational states of a bacterial α2-macroglobulin resemble those of human complement C3.Pyrococcus horikoshii TET2 peptidase assembling process and associated functional regulation.Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase.Intrinsic disorder in measles virus nucleocapsids.Protein dynamics studied by neutron scattering.Low resolution structure of a bacterial SLC26 transporter reveals dimeric stoichiometry and mobile intracellular domainsNeutron scattering reveals extremely slow cell water in a Dead Sea organism.Dynamical coupling of intrinsically disordered proteins and their hydration water: comparison with folded soluble and membrane proteinsLow-resolution structure of vaccinia virus DNA replication machineryTime-resolved neutron scattering provides new insight into protein substrate processing by a AAA+ unfoldaseOn the quest for the elusive mechanism of action of daptomycin: Binding, fusion, and oligomerization.TET peptidases: A family of tetrahedral complexes conserved in prokaryotes.Small-Angle Neutron Scattering for Structural Biology of Protein-RNA Complexes.SAXS/SANS on Supercharged Proteins Reveals Residue-Specific Modifications of the Hydration ShellNeutron scattering: a tool to detect in vivo thermal stress effects at the molecular dynamics level in micro-organisms.Characterization of a pre-export enzyme-chaperone complex on the twin-arginine transport pathway.The influence of solvent composition on global dynamics of human butyrylcholinesterase powders: a neutron-scattering study.Conserved structure and domain organization among bacterial Slc26 transporters.2017 publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution: an update.Translational diffusion of hydration water correlates with functional motions in folded and intrinsically disordered proteins.Effects of soman inhibition and of structural differences on cholinesterase molecular dynamics: a neutron scattering study.Assessing the conformational changes of pb5, the receptor-binding protein of phage T5, upon binding to its Escherichia coli receptor FhuA.Dynamics of hydration water in deuterated purple membranes explored by neutron scattering.Direct correlation between molecular dynamics and enzymatic stability: a comparative neutron scattering study of native human butyrylcholinesterase and its "aged" soman conjugate.Molecular adaptation and salt stress response of Halobacterium salinarum cells revealed by neutron spectroscopy.From shell to cell: neutron scattering studies of biological water dynamics and coupling to activity.A simple procedure to evaluate the efficiency of bio-macromolecular rigid-body refinement by small-angle scattering.A structure refinement protocol combining NMR residual dipolar couplings and small angle scattering restraints.Combining NMR and small angle X-ray and neutron scattering in the structural analysis of a ternary protein-RNA complex.Characterization of the elongasome core PBP2 : MreC complex of Helicobacter pylori.The low-temperature inflection observed in neutron scattering measurements of proteins is due to methyl rotation: direct evidence using isotope labeling and molecular dynamics simulations.
P50
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P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Frank Gabel
@ast
Frank Gabel
@en
Frank Gabel
@es
Frank Gabel
@nl
Frank Gabel
@sl
type
label
Frank Gabel
@ast
Frank Gabel
@en
Frank Gabel
@es
Frank Gabel
@nl
Frank Gabel
@sl
prefLabel
Frank Gabel
@ast
Frank Gabel
@en
Frank Gabel
@es
Frank Gabel
@nl
Frank Gabel
@sl
P106
P1153
15831814800
P21
P31
P496
0000-0003-3446-2601