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Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion StudyRapid Determination of Fast Protein Dynamics from NMR Chemical Exchange Saturation Transfer DataMeasurement of histidine pKa values and tautomer populations in invisible protein states.Quantifying millisecond exchange dynamics in proteins by CPMG relaxation dispersion NMR using side-chain 1H probes.Characterizing RNA dynamics at atomic resolution using solution-state NMR spectroscopyKinetic Cooperativity in Human Pancreatic Glucokinase Originates from Millisecond Dynamics of the Small Domain.Characterizing slow chemical exchange in nucleic acids by carbon CEST and low spin-lock field R(1ρ) NMR spectroscopy.Characterizing complex dynamics in the transactivation response element apical loop and motional correlations with the bulge by NMR, molecular dynamics, and mutagenesisThe role of ligands on the equilibria between functional states of a G protein-coupled receptor.Synthesis of 6-phosphofructose aspartic acid and some related Amadori compounds.Residue-Specific Interactions of an Intrinsically Disordered Protein with Silica Nanoparticles and their Quantitative Prediction.Absolute Minimal Sampling in High-Dimensional NMR Spectroscopy.Probing slowly exchanging protein systems via ¹³Cα-CEST: monitoring folding of the Im7 protein.Dynamics of large elongated RNA by NMR carbon relaxation.Insight into the CSA tensors of nucleobase carbons in RNA polynucleotides from solution measurements of residual CSA: towards new long-range orientational constraints.The Michaelis Complex of Arginine Kinase Samples the Transition State at a Frequency That Matches the Catalytic Rate.Absolute Minimal Sampling of Homonuclear 2D NMR TOCSY Spectra for High-Throughput Applications of Complex Mixtures.Resonance assignments of wild-type and two cysteine-free variants of the four-helix bundle protein, RopQuantitative Binding Behavior of Intrinsically Disordered Proteins to Nanoparticle Surfaces at Individual Residue Level1H, 13C, 15N resonance assignment of recombinant Euplotes raikovi protein Er-23Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groupsExtending the Range of Microsecond-to-Millisecond Chemical Exchange Detected in Labeled and Unlabeled Nucleic Acids by Selective Carbon R1ρNMR SpectroscopyPulsed field gradient NMR investigation of solubilization equilibria in amino acid and dipeptide terminated micellar and polymeric surfactant solutionsFunctional protein dynamics on uncharted time scales detected by nanoparticle-assisted NMR spin relaxation
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Q27666244-6B9C7E46-ABB6-4BE7-A425-37593349D0EEQ31040837-A6C65FCB-0966-4FF8-9B13-EAA96588F2AFQ33674477-F0DD768B-26FE-4CB6-BA11-B8A4F3F2DE8CQ34148956-4A8E3037-6F6A-4BEC-8D12-0EAECBC21CB7Q35872584-AF531BAE-D4F5-4DDE-815C-68489C6E0772Q36104359-37F5B765-E3A7-4506-88E6-F0CC5993F1F5Q36584750-C61118F3-3729-4021-8403-00176C1C9371Q36908415-31EA76E3-9AE5-48BF-AB62-4A0CADC1AD26Q37149545-ED8EA31B-79B1-4CB7-9AB2-AFA47988AB16Q41972545-4C472DCB-B3E6-406F-9714-4D13854719F1Q43163854-7A799C17-696D-4F7F-8076-0F72B120E552Q43529522-64DA1B7F-093F-4225-A214-717D0E8C1C0FQ43790145-29EAFEC9-F50F-43B8-9873-01BB531A7759Q46875431-9066413B-5A0B-4585-96F3-F9857B95EA86Q46907440-3B58A1F3-8ADB-4195-949D-42B41156B777Q48045242-32D8A4A9-8EEF-45B8-A5E5-E5034ED717FEQ48096339-F812BA4D-202C-4469-A817-74127B566E1AQ58480005-86FB376A-9C7C-4F49-A73E-DA63E1BB2F71Q58480008-73DC6814-249D-47D9-8122-D900B1DCC7BAQ58480011-A65111DF-82BE-40B7-B2C1-DF81FDFBB627Q58480041-1B299330-95C5-44A4-B56A-15C861576818Q58480044-336927CB-72A8-4D34-944C-368F96274AA7Q58480048-3C7F9AC2-3BC1-488C-8DB8-DBDCABCE7912Q92894083-748A1315-7AC2-42F5-9C63-2DFA72E19823
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description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Alexandar L Hansen
@ast
Alexandar L Hansen
@en
Alexandar L Hansen
@es
Alexandar L Hansen
@nl
type
label
Alexandar L Hansen
@ast
Alexandar L Hansen
@en
Alexandar L Hansen
@es
Alexandar L Hansen
@nl
prefLabel
Alexandar L Hansen
@ast
Alexandar L Hansen
@en
Alexandar L Hansen
@es
Alexandar L Hansen
@nl
P106
P31
P496
0000-0003-4474-7141