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Detecting O2 binding sites in protein cavitiesThe solution structure of the MANEC-type domain from hepatocyte growth factor activator inhibitor-1 reveals an unexpected PAN/apple domain-type foldLong unfolded linkers facilitate membrane protein import through the nuclear pore complex.Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion.Studying excited states of proteins by NMR spectroscopy.The solution structure, binding properties, and dynamics of the bacterial siderophore-binding protein FepBNMR chemical shift data and ab initio shielding calculations: emerging tools for protein structure determination.Cavity as a source of conformational fluctuation and high-energy state: high-pressure NMR study of a cavity-enlarged mutant of T4 lysozymeNear-complete 1H, 13C, 15N resonance assignments of dimethylsulfoxide-denatured TGFBIp FAS1-4 A546T.Probing microsecond time scale dynamics in proteins by methyl (1)H Carr-Purcell-Meiboom-Gill relaxation dispersion NMR measurements. Application to activation of the signaling protein NtrC(r)Cystathionine β-synthase (CBS) domains 1 and 2 fulfill different roles in ionic strength sensing of the ATP-binding cassette (ABC) transporter OpuA.Structural basis for RNA-genome recognition during bacteriophage Qβ replication.Using NMR chemical shifts to calculate the propensity for structural order and disorder in proteins.Contemporary NMR Studies of Protein Electrostatics.Aspartate buffer and divalent metal ions affect oxytocin in aqueous solution and protect it from degradation.How epigallocatechin gallate can inhibit α-synuclein oligomer toxicity in vitro.Bicyclic peptide inhibitor of urokinase-type plasminogen activator: mode of action.Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3.Comprehensive determination of protein tyrosine pKa values for photoactive yellow protein using indirect 13C NMR spectroscopy.pK(a) values for side-chain carboxyl groups of a PGB1 variant explain salt and pH-dependent stabilityOptimized co-solute paramagnetic relaxation enhancement for the rapid NMR analysis of a highly fibrillogenic peptide.(1)H, (13)C, and (15)N resonance assignment of photoactive yellow protein.Comprehensive determination of (3)J (HNHalpha) for unfolded proteins using (13)C'-resolved spin-echo difference spectroscopy.ncIDP-assign: a SPARKY extension for the effective NMR assignment of intrinsically disordered proteins.Is pressure-induced signal loss in NMR spectra for the Leu99Ala cavity mutant of T4 lysozyme due to unfolding?Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme.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.Nuclear magnetic resonance-based determination of dioxygen binding sites in protein cavities.Conformation and dynamics of ribosomal stalk protein L12 in solution and on the ribosome.Unambiguous Determination of Protein Arginine Ionization States in Solution by NMR Spectroscopy.Special issue as a tribute to Lewis E Kay on his 50th birthday.Aberrant increase of NMR signal in hydrogen exchange experiments. Observation and explanation.Aβ dimers differ from monomers in structural propensity, aggregation paths and population of synaptotoxic assemblies.Easy and unambiguous sequential assignments of intrinsically disordered proteins by correlating the backbone 15N or 13C' chemical shifts of multiple contiguous residues in highly resolved 3D spectra.Narrowing the gap between experimental and computational determination of methyl group dynamics in proteinsElectrostatic Contributions to Residue-Specific Protonation Equilibria and Proton Binding Capacitance for a Small Protein†Latent and active p53 are identical in conformationAssignment of 1H(N), 15N, 13C(alpha), 13CO and 13C(beta) resonances in a 67 kDa p53 dimer using 4D-TROSY NMR spectroscopyProtein Surface and Core Dynamics Show Concerted Hydration-Dependent ActivationAccurate Methyl Group Dynamics in Protein Simulations with AMBER Force Fields
P50
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P50
description
researcher ORCID ID = 0000-0001-9427-8406
@en
wetenschapper
@nl
name
Frans A.A. Mulder
@ast
Frans A.A. Mulder
@en
Frans A.A. Mulder
@es
Frans A.A. Mulder
@nl
type
label
Frans A.A. Mulder
@ast
Frans A.A. Mulder
@en
Frans A.A. Mulder
@es
Frans A.A. Mulder
@nl
prefLabel
Frans A.A. Mulder
@ast
Frans A.A. Mulder
@en
Frans A.A. Mulder
@es
Frans A.A. Mulder
@nl
P106
P1153
7005050052
P31
P496
0000-0001-9427-8406