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High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopyPre-fibrillar alpha-synuclein variants with impaired beta-structure increase neurotoxicity in Parkinson's disease models3D structure determination of the Crh protein from highly ambiguous solid-state NMR restraintsEngineering amyloid-like assemblies from unstructured peptides via site-specific lipid conjugationConformational Plasticity of the POTRA 5 Domain in the Outer Membrane Protein Assembly Factor BamA.Magic-angle-spinning solid-state NMR of membrane proteins.Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach.Solid-state NMR studies of full-length BamA in lipid bilayers suggest limited overall POTRA mobility.Proton clouds to measure long-range contacts between nonexchangeable side chain protons in solid-state NMR.Molecular Mechanism of Overhauser Dynamic Nuclear Polarization in Insulating Solids.A concept for rapid protein-structure determination by solid-state NMR spectroscopy.Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy.Characterization of membrane protein function by solid-state NMR spectroscopy.An Efficient Labelling Approach to Harness Backbone and Side-Chain Protons in (1) H-Detected Solid-State NMR Spectroscopy.Biomolecular NMR: recent advances in liquids, solids and screening.Overhauser effects in insulating solidsEfficient Dynamic Nuclear Polarization at 800 MHz/527 GHz with Trityl-Nitroxide Biradicals.Probing conformational disorder in neurotensin by two-dimensional solid-state NMR and comparison to molecular dynamics simulations(1) H-Detected Solid-State NMR Studies of Water-Inaccessible Proteins In Vitro and In Situ.A Two-Tailed Phosphopeptide Crystallizes to Form a Lamellar Structure.Amyloid-like interactions within nucleoporin FG hydrogels.Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR.Dynamic nuclear polarization NMR spectroscopy: revealing multiple conformations in lipid-anchored peptide vaccines.Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR.Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein.Sequence-independent control of peptide conformation in liposomal vaccines for targeting protein misfolding diseases.Bacteriophage SPP1 tail tube protein self-assembles into β-structure-rich tubes.High-resolution solid-state NMR applied to polypeptides and membrane proteins.Cellular solid-state nuclear magnetic resonance spectroscopyInvestigation of ligand-receptor systems by high-resolution solid-state NMR: recent progress and perspectives.Hydrogen bond strength in membrane proteins probed by time-resolved (1)H-detected solid-state NMR and MD simulations.Molecular interactions investigated by multi-dimensional solid-state NMR.Structural constraints for the Crh protein from solid-state NMR experiments.Magic-angle-spinning NMR spectroscopy applied to small molecules and peptides in lipid bilayers.Shape Control of Colloidal Cu2-x S Polyhedral Nanocrystals by Tuning the Nucleation RatesSolid-state NMR-based approaches for supramolecular structure elucidation.Disaccharides impact the lateral organization of lipid membranes.EGFR Dynamics Change during Activation in Native Membranes as Revealed by NMR.A tailored multi-frequency EPR approach to accurately determine the magnetic resonance parameters of dynamic nuclear polarization agents: application to AMUPol.A DNP-supported solid-state NMR study of carbon species in fluid catalytic cracking catalysts.
P50
Q21562552-E361D625-6B06-4B36-99AE-8DCBCD16867BQ24315670-7018D715-0F84-486E-AAE7-E9065349EA37Q27649879-81AE9923-C522-4044-B628-8ADB3D302357Q28542905-EDC2451A-5BD5-4824-857D-2EB7EE014A2DQ30152919-99FA034C-23D1-4A18-BAA3-3943033D73ECQ30152937-D8262715-0BA1-4B9B-AFA6-2D56574BEB0CQ30153258-3B7DD917-6D63-4626-BF3B-952476DDFD97Q30153432-C9BBF6C9-1C82-429A-8DAF-EE7E72F725FBQ30153443-37F8DAE6-84C8-488C-979D-769C48A23169Q30313222-63356267-1E6A-439D-8C5D-2D7C7BC893B2Q30350304-C1A95248-0B3B-4BA6-A3AB-7F3B527008B9Q30351384-8E9DCE8C-28E9-473B-BA9F-1E1C5C9888D6Q30362895-836D8136-7803-4F98-8627-6BAEB7A83246Q30381228-842F262B-46DD-4A31-BEE3-09D938A0A58FQ30784657-52F1F9F4-1FED-48D6-9982-96F6FEB68FACQ30843453-1E531E55-5C1D-41D5-B31C-86E527A97BD9Q30987014-005320DC-B4E4-4913-99AF-1E438C334381Q30993418-3A673E15-6DA1-4B72-979D-C1D2FD043209Q31133280-43B6CB6E-34F7-4BDE-8A8C-7E583604C3A5Q31161455-54F93913-E38B-4864-B13D-4B8E227779C9Q33778932-41A5EBA5-4279-41A7-96DB-9BCF404B4486Q34115959-FD272744-8E72-4BB3-9472-4BAC11241065Q34371373-B0B8F0B8-6C65-4029-AA7A-E1F3C40C9D60Q34513469-C929DAFF-6F43-48F7-BAED-5326A04EF3D1Q34667737-6A9D480A-4199-4F72-A834-6E3302809F45Q34799960-4260823F-79F8-472B-B21D-0A518BCD9585Q35055657-D4207951-C944-40E9-AABE-09D10FEEDA6EQ35586094-0BC4E46B-C71F-4069-A681-75C32A6B1040Q35882349-21895ABC-6F5A-4302-A4C8-3169EA44BE8CQ36153035-B0E257BA-7102-44B1-BF88-EC5E30E64734Q36323076-6E414220-7C11-4E58-982F-D3EBFDBF394EQ36581847-46893C7F-A7E6-4CD5-8894-7778F4F589CBQ36964137-0A574772-4FFF-4B0A-8543-AF070758CF18Q36979508-54F51910-59A8-4421-9BBD-F809FA329610Q37303717-E16BB2DF-6045-4D8C-A2E3-AD316E151D08Q38099050-10CFD6CB-B1AF-48E3-8F0D-636756809C41Q38303505-17227B25-C13F-40D2-97F2-46B4F291C583Q38731480-C5493E15-EC6A-4B21-BA41-12C0F73C14F1Q38769095-A53D5989-DD9F-4EC5-9C57-9FC74BE2279EQ38887532-9737C5C9-3342-4658-950B-020CCF2EE504
P50
description
German physicist and academic
@en
academisch docent
@nl
հետազոտող
@hy
name
Marc Baldus
@ast
Marc Baldus
@en
Marc Baldus
@es
Marc Baldus
@nl
Marc Baldus
@sl
type
label
Marc Baldus
@ast
Marc Baldus
@en
Marc Baldus
@es
Marc Baldus
@nl
Marc Baldus
@sl
altLabel
Baldus M
@en
M. Baldus
@nl
prefLabel
Marc Baldus
@ast
Marc Baldus
@en
Marc Baldus
@es
Marc Baldus
@nl
Marc Baldus
@sl
P106
P1006
P214
P227
P1006
P1053
C-2737-2009
P1153
7004926277
P21
P213
0000 0001 3967 3796
P214
P227
P2381
P2798
P31
P3829
P4012
P496
0000-0001-7068-5613
P569
1967-11-28T00:00:00Z