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Analysis of the Intrinsically Disordered N-Terminus of the DNA Junction-Resolving Enzyme T7 Endonuclease I: Identification of Structure Formed upon DNA BindingThe histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexesStructural plasticity of histones H3-H4 facilitates their allosteric exchange between RbAp48 and ASF1The spatial effect of protein deuteration on nitroxide spin-label relaxation: implications for EPR distance measurementThe histone chaperones Nap1 and Vps75 bind histones H3 and H4 in a tetrameric conformationThe use of the Rx spin label in orientation measurement on proteins, by EPR.DEER Sensitivity between Iron Centers and Nitroxides in Heme-Containing Proteins Improves Dramatically Using Broadband, High-Field EPR.The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution.Cryo-EM Structure of a Relaxase Reveals the Molecular Basis of DNA Unwinding during Bacterial Conjugation.Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes.EPR spectroscopy of a family of Cr(III) 7M(II) (M = Cd, Zn, Mn, Ni) "wheels": studies of isostructural compounds with different spin ground states.EPR Distance Measurements in Deuterated Proteins.Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosomeDistance Measurement of a Noncovalently Bound Y@C82 Pair with Double Electron Electron Resonance SpectroscopyDistance determination in heterogeneous DNA model systems by pulsed EPRThe use of composite pulses for improving DEER signal at 94GHzAllosteric activation of an ion channel triggered by modification of mechanosensitive nano-pocketsA Gadolinium Spin Label with Both a Narrow Central Transition and Short Tether for Use in Double Electron Electron Resonance Distance Measurements
P50
Q27301695-A049D983-B8CC-4A2E-9244-799EDBF2D0B9Q27704509-D94796B7-50AE-4164-AFCF-358BF2FE59F8Q30531468-3331D611-66AB-459B-BC20-988ECD4DFA2AQ30602280-9CEC8A5D-B015-4A6C-A013-A2168BE0B5EBQ34978251-03773D6C-DF26-4F68-9946-CB9FB35C5C75Q36587544-5324C389-CAAF-4359-BA9C-07C4602A9C66Q36890068-C3824D61-FED4-42D7-A9D3-3DEF86AA6599Q39769792-1ED9E9C7-1B4D-42C9-B919-62E89D4A7135Q41598108-6A424E66-CAD0-4EC7-B3AA-6A4DCB66EEF5Q41850902-C719696D-C5FB-4A6D-B8A8-F9B59CC9EF78Q51852732-957A8249-4FD7-4194-890D-67E845FC3111Q53313337-24EDCA6A-EEB6-44B0-BB08-C4912C0685B9Q56530225-B94E8C4C-D558-4001-9A66-9E9211848F18Q59455390-02DA5D84-0158-4AE8-B754-D26A18118C87Q81334683-22728ED9-A29A-4BAF-893D-4009708D04E2Q87817933-E5714BB4-5D86-4C86-867D-B1FC0DCC697DQ90640032-D1935850-6504-4B07-B064-87E64BB9CF59Q91677056-4CF01EAD-8048-4EF7-9946-56560B469EC1
P50
description
investigador
@es
researcher
@en
wetenschapper
@nl
name
Hassane El-Mkami
@en
Hassane El-Mkami
@nl
type
label
Hassane El-Mkami
@en
Hassane El-Mkami
@nl
prefLabel
Hassane El-Mkami
@en
Hassane El-Mkami
@nl
P31
P496
0000-0002-0552-5784