about
Crystal structure of tryptophan hydroxylase with bound amino acid substrateCrystal structures of the all-cysteinyl-coordinated D14C variant of Pyrococcus furiosus ferredoxin: [4Fe-4S] ↔ [3Fe-4S] cluster conversionA new insight into the zinc-dependent DNA-cleavage by the colicin E7 nuclease: a crystallographic and computational studyThe crystal structure of human dopamine β-hydroxylase at 2.9 Å resolutionExpression and characterization of recombinant Rhodocyclus tenuis high potential iron-sulfur protein.Fine tuning of the catalytic activity of colicin E7 nuclease domain by systematic N-terminal mutations.Crystallization and preliminary crystallographic analysis of an Escherichia coli-selected mutant of the nuclease domain of the metallonuclease colicin E7.The antimalarial drug quinine interferes with serotonin biosynthesis and action.Extracellular polymeric substances are transient media for microbial extracellular electron transfer.Stabilization of tryptophan hydroxylase 2 by l-phenylalanine-induced dimerization.In situ STM imaging and direct electrochemistry of Pyrococcus furiosus ferredoxin assembled on thiolate-modified Au111 surfaces.Expression, purification and enzymatic characterization of the catalytic domains of human tryptophan hydroxylase isoforms.The role of the N-terminal loop in the function of the colicin E7 nuclease domain.Electrochemical single-molecule AFM of the redox metalloenzyme copper nitrite reductase in action.Substrate binding activates the designed triple mutant of the colicin E7 metallonuclease.Histidine side-chain dynamics and protonation monitored by 13C CPMG NMR relaxation dispersion.Characterization of conformational exchange of a histidine side chain: protonation, rotamerization, and tautomerization of His61 in plastocyanin from Anabaena variabilis.Weak self-association of human growth hormone investigated by nitrogen-15 NMR relaxation.Kinetics and mechanism of the acid transition of the active site in plastocyanin.Isoform-Specific Substrate Inhibition Mechanism of Human Tryptophan Hydroxylase.The 1.5 A resolution crystal structure of [Fe3S4]-ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus.Arabidopsis profilins are functionally similar to yeast profilins: identification of a vascular bundle-specific profilin and a pollen-specific profilin.Cloning and characterisation of the gene encoding cytochrome c4 from Pseudomonas stutzeri.Chemical Approach to Biological Safety: Molecular-Level Control of an Integrated Zinc Finger Nuclease.An efficient arabinoxylan-debranching α-L-arabinofuranosidase of family GH62 from Aspergillus nidulans contains a secondary carbohydrate binding site.Computational chemistry of modified [MFe3S4] and [M2Fe2S4] clusters: assessment of trends in electronic structure and properties.Advanced purification strategy for CueR, a cysteine containing copper(I) and DNA binding protein.Electron transfer patterns of the di-heme protein cytochrome c(4) from Pseudomonas stutzeri.Structure of plastocyanin from the cyanobacterium Anabaena variabilis.Side Effect of Good's Buffers on Optical Properties of Gold Nanoparticle SolutionsInactivation of barley limit dextrinase inhibitor by thioredoxin-catalysed disulfide reductionEfficient secretory expression of functional barley limit dextrinase inhibitor by high cell-density fermentation of Pichia pastorisOn the use of pseudocontact shifts in the structure determination of metalloproteinsEffects of NO2-modification of Tyr83 on the reactivity of spinach plastocyanin with cytochrome fRole of nucleotide exchange and hydrolysis in the function of profilin in action assemblyTotal synthesis of a miniferredoxinProfilin plays a role in cell elongation, cell shape maintenance, and flowering in ArabidopsisCrystallization and preliminary crystallographic investigations of cytochrome c4 from Pseudomonas stutzeriIsolation and purification of plastocyanin from spinach stored frozen using hydrophobic interaction and ion-exchange chromatographyA new procedure for fast isolation and purification of plastocyanin from the cyanobacterium Anabaena variabilis
P50
Q27652575-B7BEE29D-8D83-4CAB-93A7-076CFAD380C4Q27667207-3785819F-523D-40C4-8D30-BF477EFC5E97Q27694911-9D4F706A-5061-482A-8B90-B5BAC2BE78E7Q28118905-3290AA01-B330-4602-8D5B-A1D46DBA953FQ33907533-AF33586D-DB60-431A-9A10-720CF5F4750DQ33977832-F5C74121-D776-4793-AF02-13B5BCFA41B7Q36865353-22901A9B-1836-422C-9C50-028F9A699278Q37453950-A7C71953-7889-4CCB-83F5-8BCCBF1069B4Q38684961-22563277-6625-4273-A260-ACB524F3D724Q41366766-518E215B-DF0A-4B54-9E4A-80B75E264A84Q42168407-9DF5140D-F9C1-4A74-8071-6318138D76EAQ43264743-F74FD1FF-020A-4855-AF2C-5C913FF518F7Q44092371-F1C51C45-5113-44F2-85E0-14E2EB9F2EAAQ44532170-D70E39C9-64B8-474E-8A3A-731F84665F53Q44780458-21B6148E-10BE-4BAB-903D-4EAE59F810FEQ45966161-638A900C-9982-4459-96B5-8FF2D667A894Q46550584-62352E23-B9F0-41F9-93C5-EDB5D8ABD26FQ46805508-662DD97B-6C03-4E3C-9BAC-4E73B177B54EQ46895125-C010F320-D3EE-4646-9BA6-8B710BA8AEADQ47648574-0DCB732D-4908-4B13-A9AD-81900659E239Q47660754-6BAC2324-D0A6-4304-9240-EB97336886F7Q48061677-8147A914-A34A-418E-A381-5560FCD7CD7DQ48081633-AC361248-F2C3-46E8-B01D-99203E54DA3DQ48114494-3C9D553A-7854-4A70-9582-D968741C798DQ48510560-ADF02F86-0EC0-434E-9EB4-05BEF726381CQ50458096-25ACB5B7-10A0-4E43-B5C0-B42DB123894EQ50864725-47F40D51-73C3-4CA8-83C6-7BABC69A366DQ51821971-24AA9797-6070-4F0E-A628-877D5647FB17Q54457168-E248FD3A-209B-4F82-B75D-4E56630D717FQ57660142-DB1C4331-65CD-4716-ADF8-73A39F0D184EQ59462221-92B42E74-DEEB-45A9-8DB9-FDA609593CBFQ59462227-2AB4E31E-06D0-41D8-BA55-55CC24CBF92DQ62126356-5113E0C0-B81F-4C56-BD0F-7FD5C4DBD03FQ67753463-12038D61-999D-444E-8649-CD543036AFEFQ71119828-5E3A66FC-94AA-4200-AD71-301054031806Q71160229-26C54B3D-DBD4-4773-A231-D4FA3826EAF3Q73294999-1DB6A084-EFC8-4BDF-A81E-F7F9D6C322A3Q80426944-B118A245-86FA-4A25-9589-4C716DB4D955Q87080574-12E715C3-3BB8-4C93-A5F4-78C521D4DAA2Q87090445-A84A8ECF-B6F0-4ABE-A313-AE2B63A627DF
P50
description
researcher ORCID ID = 0000-0002-9540-8679
@en
wetenschapper
@nl
name
Hans Erik Mølager Christensen
@ast
Hans Erik Mølager Christensen
@en
Hans Erik Mølager Christensen
@es
Hans Erik Mølager Christensen
@nl
type
label
Hans Erik Mølager Christensen
@ast
Hans Erik Mølager Christensen
@en
Hans Erik Mølager Christensen
@es
Hans Erik Mølager Christensen
@nl
prefLabel
Hans Erik Mølager Christensen
@ast
Hans Erik Mølager Christensen
@en
Hans Erik Mølager Christensen
@es
Hans Erik Mølager Christensen
@nl
P1153
24758059500
P31
P496
0000-0002-9540-8679