about
The role of protein-bound water molecules in microbial rhodopsinsDirectional proton transfer in membrane proteins achieved through protonated protein-bound water molecules: a proton diodeCatalytic mechanism of a mammalian Rab{middle dot}RabGAP complex in atomic detailStructural basis of slow activation gating in the cardiac I Ks channel complexpKa calculations suggest storage of an excess proton in a hydrogen-bonded water network in bacteriorhodopsinSurface-Attached Polyhistidine-Tag Proteins Characterized by FTIR Difference SpectroscopyA method for the comparison of multi-platform spectral histopathology (SHP) data sets.Monitoring protein-ligand interactions by time-resolved FTIR difference spectroscopy.Proton binding within a membrane protein by a protonated water clusterA delocalized proton-binding site within a membrane proteinThe structure of active opsin as a basis for identification of GPCR agonists by dynamic homology modelling and virtual screening assays.In channelrhodopsin-2 Glu-90 is crucial for ion selectivity and is deprotonated during the photocycle.Coupling of light-induced electron transfer to proton uptake in photosynthesis.A phosphoryl transfer intermediate in the GTPase reaction of Ras in complex with its GTPase-activating proteinProton transfer via a transient linear water-molecule chain in a membrane protein.A modified infrared spectrometer with high time resolution and its application for investigating fast conformational changes of the GTPase Ras.Single cell analysis/data handling: general discussion.Proteins in action monitored by time-resolved FTIR spectroscopy.Ras and GTPase-activating protein (GAP) drive GTP into a precatalytic state as revealed by combining FTIR and biomolecular simulations.The GAP arginine finger movement into the catalytic site of Ras increases the activation entropyStructural changes of membrane-anchored native PrP(C)De novo design of conformationally flexible transmembrane peptides driving membrane fusion.The dynamics of the catalytic site in small GTPases, variations on a common motif.What vibrations tell us about GTPases.In vitro prediction of the efficacy of molecularly targeted cancer therapy by Raman spectral imaging.Colocalization of fluorescence and Raman microscopic images for the identification of subcellular compartments: a validation study.Elucidation of Single Hydrogen Bonds in GTPases via Experimental and Theoretical Infrared Spectroscopy.Label-free imaging of drug distribution and metabolism in colon cancer cells by Raman microscopy.It's in your blood: spectral biomarker candidates for urinary bladder cancer from automated FTIR spectroscopy.Unravelling the mechanism of dual-specificity GAPs.Dynamics of water molecules in the bacteriorhodopsin trimer in explicit lipid/water environment.Exploring the Multidimensional Free Energy Surface of Phosphoester Hydrolysis with Constrained QM/MM Dynamics.The assignment of the different infrared continuum absorbance changes observed in the 3000-1800-cm(-1) region during the bacteriorhodopsin photocycle.Theoretical IR spectroscopy based on QM/MM calculations provides changes in charge distribution, bond lengths, and bond angles of the GTP ligand induced by the Ras-protein.Light-induced reactions of Escherichia coli DNA photolyase monitored by Fourier transform infrared spectroscopy.Catalysis of GTP hydrolysis by small GTPases at atomic detail by integration of X-ray crystallography, experimental, and theoretical IR spectroscopy.Marker-free automated histopathological annotation of lung tumour subtypes by FTIR imaging.Time-resolved Fourier transform infrared spectroscopy of the nucleotide-binding domain from the ATP-binding Cassette transporter MsbA: ATP hydrolysis is the rate-limiting step in the catalytic cycle.The role of magnesium for geometry and charge in GTP hydrolysis, revealed by quantum mechanics/molecular mechanics simulations.N-Ras forms dimers at POPC membranes.
P50
Q26823393-1A5F0E79-75AB-4FC2-BC5E-EBC3A8A5F893Q27663829-4755092D-1509-4789-A24E-77D39DF491DCQ27675470-B5A2ADE7-3ED3-422C-A0B3-5FE45697A907Q28241288-AAA5019E-E761-4F7E-A2D5-4179404B04B0Q29396104-BFE4CF83-1DD4-4BE7-B770-2BF236E688F1Q30050269-219DBCBD-0F65-42E7-9A0F-4EADAA487C4DQ30890356-EB50C610-F0AF-4F5B-BDC4-8C83D39C6E86Q33216584-A2307156-19DA-4589-96E6-F848D4C1CAA4Q33928561-F80107C8-92EF-4E36-A52A-13E73875FDDDQ33990967-FFF8DA7C-A035-48FF-BC7E-0C6F79FC47C1Q34057838-DCA01793-A499-42CC-8F34-028105C761D9Q34118883-B06A0308-F238-4546-8159-4768715A041EQ34215741-B143C86B-40AA-4573-AC74-235B236D84B1Q35080333-C47CE205-2E79-44EC-84BC-52FF1F8657A7Q35105201-B8BB48B8-7FAA-4229-B358-AB36484F0329Q35205534-FCFB34DB-F850-43AC-8F86-5789785ADBEBQ36047346-6188EBF0-414D-42C9-9D54-8D8938E905C4Q36122187-E32DA854-804E-4FD5-972B-1A8BE52AACACQ36279979-EDA81406-6DF0-41FD-89F9-F77563F799E2Q36609155-52EB62EB-ED6F-46BD-966D-7CA7960869A2Q36825306-774F4024-E660-4B70-8332-32E93A26C553Q37571104-71EE4B4F-CC78-4D6C-9D97-D94007D85C3DQ38107679-B60410D2-9F91-4E11-924B-0B6797ED596FQ38242876-4E4B9347-DCF0-4D85-B501-39B4679C07F1Q38853649-E9F9BB6F-3F22-4048-9623-B8E1F19FCF0DQ38909985-E11E4E7C-EE34-4892-8AB7-D1BFAC6B4EEAQ39026741-6BA39CE1-3523-4A73-8E4B-A335DE25C744Q39034201-C23C9697-FC73-49A7-8891-2EC505FD3A84Q39278631-21287412-9E47-4479-B1C0-1EEEE5717F76Q40117233-5465CA91-0FED-4800-AED5-8E6FCBE3F059Q40272621-645917D0-BAFB-48C2-8699-CD030B4B52C0Q40290811-3728A615-65AD-41CB-8500-87F011E087DCQ40300054-D656ABBA-551F-4FC9-9FC9-0933E7813BCFQ40334259-4C20C569-7F16-4109-A8DE-A8968E0AA283Q40431921-743EB31A-F4B4-48BB-996A-F228B99FB2C3Q41456819-D889B3CD-543A-4859-ACE8-C1202D45B9DDQ41662930-52C2BE64-F63F-4D4A-81C6-8A1CF35EC74AQ41997470-6A8647F6-4F52-4741-BFBD-33C0063AE91EQ42243109-F7D71023-03E9-49C8-9FD1-5F3951FAD816Q42425935-3D36A429-6DBF-4279-B5D9-3533E8B3B61C
P50
description
natuurkundige
@nl
researcher ORCID ID = 0000-0001-8759-5964
@en
name
Klaus Gerwert
@ast
Klaus Gerwert
@en
Klaus Gerwert
@es
Klaus Gerwert
@nl
type
label
Klaus Gerwert
@ast
Klaus Gerwert
@en
Klaus Gerwert
@es
Klaus Gerwert
@nl
prefLabel
Klaus Gerwert
@ast
Klaus Gerwert
@en
Klaus Gerwert
@es
Klaus Gerwert
@nl
P214
P227
P19
P21
P214
P227
P31
P496
0000-0001-8759-5964
P569
1956-01-01T00:00:00Z
P735
P7859
viaf-160550522