about
Reaction Mechanism of N -Acetylneuraminic Acid Lyase Revealed by a Combination of Crystallography, QM/MM Simulation, and MutagenesisThe basis for carbapenem hydrolysis by class A β-lactamases: a combined investigation using crystallography and simulationsThe Catalytic Mechanism of a Natural Diels-Alderase Revealed in Molecular DetailStructure and Function in Homodimeric Enzymes: Simulations of Cooperative and Independent Functional Motions.Structural and dynamic properties of the human prion protein.Dynameomics: a comprehensive database of protein dynamics.Diverse effects on the native β-sheet of the human prion protein due to disease-associated mutations.Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding.Influence of pH on the human prion protein: insights into the early steps of misfolding.Biomolecular simulation and modelling: status, progress and prospects.The consequences of pathogenic mutations to the human prion protein.Computational enzymology: insight into biological catalysts from modelling.Molecular dynamics as an approach to study prion protein misfolding and the effect of pathogenic mutations.Combined quantum mechanics/molecular mechanics (QM/MM) methods in computational enzymology.Atomistic non-adiabatic dynamics of the LH2 complex with a GPU-accelerated ab initio exciton model.QM/MM simulations as an assay for carbapenemase activity in class A β-lactamases.How Static Disorder Mimics Decoherence in Anisotropy Pump-Probe Experiments on Purple-Bacteria Light Harvesting Complexes.Simulations of membrane-bound diglycosylated human prion protein reveal potential protective mechanisms against misfolding.Comparison of ab Initio, DFT, and Semiempirical QM/MM Approaches for Description of Catalytic Mechanism of Hairpin Ribozyme.Structural Basis of Catalysis in the Bacterial Monoterpene Synthases Linalool Synthase and 1,8-Cineole Synthase.Identification of the quinolinedione inhibitor binding site in Cdc25 phosphatase B through docking and molecular dynamics simulations.Testing high-level QM/MM methods for modeling enzyme reactions: acetyl-CoA deprotonation in citrate synthase.Affinity of Avr2 for tomato cysteine protease Rcr3 correlates with the Avr2-triggered Cf-2-mediated hypersensitive response.QM/MM modelling of ketosteroid isomerase reactivity indicates that active site closure is integral to catalysis.Conformational change and ligand binding in the aristolochene synthase catalytic cycle.Comparison of different quantum mechanical/molecular mechanics boundary treatments in the reaction of the hepatitis C virus NS3 protease with the NS5A/5B substrate.High-level QM/MM modelling predicts an arginine as the acid in the condensation reaction catalysed by citrate synthase.Quantum Mechanics/Molecular Mechanics Simulations Identify the Ring-Opening Mechanism of Creatininase.Dynameomics: protein dynamics and unfolding across fold space.Enzymatic synthesis of natural (+)-aristolochene from a non-natural substrate.Rapid Estimation of Catalytic Efficiency by Cumulative Atomic Multipole Moments: Application to Ketosteroid Isomerase Mutants.Dynamical origins of heat capacity changes in enzyme-catalysed reactions.Multiscale analysis of enantioselectivity in enzyme-catalysed 'lethal synthesis' using projector-based embedding.A Projector-Embedding Approach for Multiscale Coupled-Cluster Calculations Applied to Citrate Synthase.On the Temperature Dependence of Enzyme-Catalyzed Rates.“Lethal Synthesis” of Fluorocitrate by Citrate Synthase Explained through QM/MM ModelingExperiment and Simulation Reveal How Mutations in Functional Plasticity Regions Guide Plant Monoterpene Synthase Product OutcomeA Multiscale Simulation Approach to Modeling Drug-Protein Binding KineticsQM/MM simulations identify the determinants of catalytic activity differences between type II dehydroquinase enzymesMultiscale Simulations of Clavulanate Inhibition Identify the Reactive Complex in Class A β-Lactamases and Predict the Efficiency of Inhibition
P50
Q27681700-A1CEBAB2-968D-42D0-ADF7-E17E0F8592E8Q27682614-AC491D47-4FAD-4465-BBAA-30CCA6A76B80Q27704810-1D88A2E4-750F-4B7C-B7A9-AB09EE54B846Q30377505-BCA9366C-64FE-481E-BE68-1376228A6ACDQ33634062-2A5EF8A3-5046-44FB-8105-96122BE83F1CQ33943177-CDB42A21-B6AA-4155-8681-7C86C6F77B59Q34293194-9920B0EE-EE0D-47AC-86B3-6AC1F33541BCQ34362290-F8068420-A24D-451E-A66E-C0D885BFAE0CQ34590614-7DA0D7E2-A889-4631-845D-5AF81DE81475Q37210701-7B088449-6513-4EFA-9247-45FCF98F40CBQ37285520-93132D04-3DB2-45EB-856A-DEA007B78171Q37333810-48A9E2A6-FEC9-4F07-B28D-D71625B309D2Q37869840-0876197D-1308-4E33-8D71-6EFF1091939CQ38096002-7C25697B-0926-473D-AD93-67F02D7310E3Q38826927-1499742D-926D-419A-918B-C4446E544469Q39112147-77838C85-575E-4CCA-9B5F-9AE042FB9433Q39305233-FDDF4573-F33C-46D1-847E-D1B9EB87164EQ40252134-3DA0BDB4-B912-466E-8107-7CE6A7EE0A1CQ40308379-25BFAB31-34F5-4BAA-9F9A-DD18B3863426Q41669615-C9756452-11D1-40A5-8E7A-58E362693D4FQ41921115-BF2B8A3A-200A-4EA3-A6C1-4180747255F5Q42944399-2192681F-F79B-44DC-93C0-57B9B87022CCQ43485716-C3B518C4-A21E-455F-BD22-DC8D10A5D7BCQ43545904-9E081F3E-6724-4263-B937-79D5DC12D111Q44033130-39290EEC-0E3A-45C9-9F35-C66720F42E3AQ45399698-DE7A8040-677E-4B95-8FFC-5322BD02DBA1Q46653476-E0FFEF93-C2E6-4467-91E8-19D5AE70C5F1Q47400568-3BF4D23A-A59F-4F08-B32E-A58FE70D8A15Q47583342-6A3DEE36-C69C-4885-A3CD-11DA71323C51Q48221298-E638C4DD-0717-4E99-8992-BD6788E9FFE2Q48334833-4E850993-0500-4E4E-850B-82E84CA03D54Q52643932-9ED93411-93BB-4D1F-A5E3-4A9DB0773208Q53080145-02F88290-3AF3-409B-8DAD-8C0BD6F14B92Q53103962-B3020213-E380-442B-B667-11FC6450459CQ53251820-E93D13CD-7FC3-492F-9400-A620E2A52846Q56626549-562E11A6-3B92-47C0-9F35-D18109C500D9Q57015738-BB472B44-9705-48A4-809C-67C6A3C19702Q57047048-742D0A70-2DB0-4851-BA02-60396393A186Q57979412-DEF1B670-0340-495B-BE0F-BBD7FDE310B4Q58456629-A5E7EFC6-ED1F-4A1E-8654-55C7B8F99F00
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Marc van der Kamp
@ast
Marc van der Kamp
@en
Marc van der Kamp
@es
Marc van der Kamp
@nl
Marc van der Kamp
@sl
type
label
Marc van der Kamp
@ast
Marc van der Kamp
@en
Marc van der Kamp
@es
Marc van der Kamp
@nl
Marc van der Kamp
@sl
prefLabel
Marc van der Kamp
@ast
Marc van der Kamp
@en
Marc van der Kamp
@es
Marc van der Kamp
@nl
Marc van der Kamp
@sl
P1053
F-6000-2013
P106
P1153
22136534400
P2002
marcvanderkamp
P21
P31
P3829
P496
0000-0002-8060-3359