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orcid.org/0000-0002-5390-3321
2024
Solid-state nuclear magnetic resonance in the structural study of polyglutamine aggregation. Van der Wel, PCA (2024) Biochemical Society Transactions, BST20230731 [DOI]
Combinations of arginine and pullulan reveal the selective effect of stabilization mechanisms on different lyophilized proteins. Nguyen et al. (2024) International Journal of Pharmaceutics, 123938 [DOI]
Photocontrol of the β-Hairpin Polypeptide Structure through an Optimized Azobenzene-Based Amino Acid Analogue. Parlato et al. (2024) J. Am. Chem. Soc. 146 (3), 2062-2071. [DOI]
2023
Anomalous peroxidase activity of cytochrome c is the primary pathogenic target in Barth syndrome. Kagan et al. (2023) Nature Metabolism 5 (12), 2184-2205. [DOI]
In situ SnSe deposition as passivation for scalable and stable quasi-2D lead–tin perovskite solar cells. Lijun Chen et al. (2023) Energy & Environmental Sci. [DOI]
Production of isotopically enriched high molecular weight hyaluronic acid and characterization by solid-state NMR. Rampratap, P.; Lasorsa, A.; Perrone, B.; Van Der Wel, P. C. A.; Walvoort, M. T. C. (2023) Carbohydrate Polymers 316: 121063 [DOI]
A Universal Nanogel‐Based Coating Approach for Medical Implant Materials. Ghosh, D., Keskin, D., Forson, A.M., Rosman, C.W.K., Bron, R., Siebenmorgen, C.M., Zu, G., Lasorsa, A., Van der Wel, P.C.A., Van Kooten, T.G., Witjes, M.J.H., Sjollema, J., Van der Mei, H.C., Van Rijn, P. (2023) Advanced NanoBiomed Research 2200141 [DOI]
New insights in polydopamine formation via surface adsorption. Hemmatpour, H., De Luca, O., Crestani, D. et al. (2023) Nature Commun. 14(1): 664 [DOI]
Fast magic angle spinning for the characterization of milligram quantities of organic and biological solids at natural isotopic abundance by 13C–13C correlation DNP-enhanced NMR. Smith et al. (2023) Solid State Nuclear Magnetic Resonance in press [DOI ] DOI: https://doi.org/10.1016/j.ssnmr.2022.101850
2022
Selective observation of semi-rigid non-core residues in dynamically complex mutant huntingtin protein fibrils. I. Matlahov, J.C. Boatz, P.C.A. van der Wel (2022) J. Struct. Biol. X. 6: 100077 [DOI ]
Binder‐free Zeolite Beta Beads with Hierarchical Porosity: Synthesis and Application as Heterogeneous Catalysts for Anisole Acylation. Zahra Asgar Pour, Romar Koelewijn, Mustapha El Hariri El Nokab, Patrick CA van der Wel, Khaled O Sebakhy, Paolo P Pescarmona (2022) ChemCatChem 14(19): e202200518 [ DOI ]
Structural Dynamics and Tunability for Colloidal Tin Halide Perovskite Nanostructures. Kushagra Gahlot, Sytze de Graaf, Herman Duim, Georgian Nedelcu, Razieh M Koushki, Majid Ahmadi, Dnyaneshwar Gavhane, Alessia Lasorsa, Oreste De Luca, Petra Rudolf, Patrick CA van der Wel, Maria A Loi, Bart J Kooi, Giuseppe Portale, Joaquín Calbo, & Loredana Protesescu (2022) Advanced Materials. 34, 2201353 [DOI]
Solid-state NMR spectroscopy insights for resolving different water pools in alginate hydrogels. Mustapha El Hariri El Nokab, Alessia Lasorsa, Khaled O Sebakhy, Francesco Picchioni, & Patrick CA van der Wel (2022) Food Hydrocolloids. 107500. [DOI].
2021
Dihedral Angle Measurements for Structure Determination by Biomolecular Solid-State NMR Spectroscopy. P.C.A. van der Wel (2021) Front Mol Biosci. 2021; 8: 791090 [DOI ]
NMR identification of a conserved Drp1 cardiolipin-binding motif essential for stress-induced mitochondrial fission. M. Mahajan, N. Bharambe, Y. Shang, B. Lu, A. Mandal, P. Madan Mohan, R. Wang, J.C. Boatz, J. Manuel Martinez Galvez, A.V. Shnyrova, X. Qi, M. Buck, P.C.A. van der Wel, & R. Ramachandran (2021) Proc Natl Acad Sci USA. 118 e2023079118. [DOI].
Regulatory inter-domain interactions influence Hsp70 recruitment to the DnaJB8 chaperone. Ryder, B.D.; Matlahov, I.; Bali, S.; Vaquer-Alicea, J.; Van der Wel, P.C.A. & Joachimiak, L.A. (2021) Nat. Commun. 12: 946 [Online]
Activation of Cytochrome C Peroxidase Function Through Coordinated Foldon Loop Dynamics upon Interaction with Anionic Lipids. Mingyue Li, Wanyang Sun, Vladimir A. Tyurin, Maria DeLucia, Jinwoo Ahn, Valerian E. Kagan, & Patrick C.A. van der Wel (2021) J. Mol. Biol., 433 (15) 167057 [DOI]
2020
Solid-state NMR studies of peripherally membrane-associated proteins: Dealing with dynamics, disorder and dilute conditions. Van der Wel, P.C.A. (2020) Chapter in “Solid-State NMR: Applications in biomembrane structure“, Editors: Frances Separovic & Marc-Antoine Sani, IOP press Biophysical Society Series [DOI]
Protofilament Structure and Supramolecular Polymorphism of Aggregated Mutant Huntingtin Exon 1. Boatz, J.C., Piretra, T., Lasorsa, A., Matlahov, I., Conway, J.F. & Van der Wel, P.C.A. (2020) J. Mol. Biol., 432(16): 4722-4744. [DOI] (Open Access)
Use of solid-state NMR spectroscopy for investigating polysaccharide-based hydrogels: A review. El Hariri El Nokab, M. & Van der Wel, P.C.A. (2020) Carbohydrate Polymers, 240: 116276. [DOI]
Redox Phospholipidomics of Enzymatically Generated Oxygenated Phospholipids as Specific Signals of Programmed Cell Death.Kagan, V. E.; Tyurina, Y. Y.; Sun, W. Y.; Vlasova, L. L.; Dar, H.; Tyurin, V. A.; Amoscato, A. A.; Mallampalli, R.; van der Wel, P. C. A.; He, R. R.; Shvedova, A.A.; Gabrilovich, D.; Bayir, H. (2020) Free Radic Biol Med, 147, 231-241. [DOI]
2019
Conformational studies of pathogenic expanded polyglutamine protein deposits from Huntington’s disease. Matlahov, I., & Van der Wel, P.C.A. (2019) Exp. Biol. Med., 244(17):1584-1595. [DOI]
Surface-Binding to Cardiolipin Nanodomains Triggers Cytochrome c Pro-apoptotic Peroxidase Activity via Localized Dynamics. Li, M., Mandal, A., Tyurin, V.A., Delucia, M., Ahn, J., Kagan, V.E., & Van der Wel, P.C.A. (2019) Structure, 27(5):806-815.e4 [URL] [DOI]
2018
Structural fingerprinting of protein aggregates by DNP-enhanced solid-state NMR at natural isotopic abundance. Smith, A.N., Märker, K., Piretra, T., Boatz, J.C., Matlahov, I., Kodali, R., Hediger, S., van der Wel, P.C.A., & De Paëpe, G. (2018) J. Am. Chem. Soc., 140(44): 14576-80 [URL] [Full-Text] [OA PDF]
Hidden motions and motion-induced invisibility: dynamics-based spectral editing in solid-state NMR. Matlahov, I., Van der Wel, P.C.A. (2018) Methods, 148: 123-135 [URL] [OA PDF]
New applications of solid-state NMR in structural biology. Van der Wel, P.C.A. (2018) Emerg. Top. Life Sci. 2, 57–67 [online] [OA PDF]
Methionine oxidized apolipoprotein A-I at the crossroads of HDL biogenesis and amyloid formation Witkowski, A., Chan, G.K.L., Boatz, J.C., Li, N.J., Inoue, A.P., Wong, J.C., Van der Wel, P.C.A., Cavigiolio, G. (2018) FASEB J. 32: 3149–3165 [online] [PubMed]
Energetics Underlying Twist Polymorphisms in Amyloid Fibrils Periole, X., Huber, T., Bonito-Oliva, A., Aberg, K.C., Van der Wel, P.C.A., Sakmar, T.P., & Marrink, S.J. (2018) J. Phys. Chem. B 122 (3), 1081-1091 [URL] [ACS reprint]
2017
Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy Van der Wel, P.C.A. (2017) Solid-state Nuclear Magnetic Resonance 88: 1-14 [URL] [Free Full Text]
Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core. Lin, H.K., Boatz, J.C., Krabbendam, I.E., Kodali, R., Hou, Z., Wetzel, R., Dolga, A.M., Poirier, M.A., and Van der Wel, P.C.A. (2017) Nature Commun. 8: 15462 [URL] [OA PDF]
Cataract-associated P23T gammaD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH. Boatz, J.C., Whitley, M.J., Li, M., Gronenborn, A.M., and Van der Wel, P.C.A. (2017) Nature Commun. 8: 15137 [DOI] [ReadCube]
On the use of ultracentrifugal devices for routine sample preparation in biomolecular magic-angle-spinning NMR. Mandal, A., Boatz, J.C., Wheeler, T., and Van der Wel, P.C.A. (2017) J. Biomol. NMR 67: 165-178 [online] [PubMed]
Backbone engineering within a latent β-hairpin structure to design inhibitors of polyglutamine amyloid formation. Kar, K., Baker, M.A., Lengyel, G.A., Hoop, C.L., Kodali, R., Byeon, I-J., Horne, W.S., Van der Wel, P.C.A., and Wetzel, R., (2017) J. Mol. Biol. 429(2), 308-323 [DOI] [PMC]
2016
MAS 1H NMR Probes Freezing Point Depression of Water and Liquid-Gel Phase Transitions in Liposomes. Mandal, A. and Van der Wel, P.C.A.* (2016) Biophys. J. 111, 1965-1973 (LINK) (DOI) ( PMC )
Peptide-directed assembly of single-helical gold nanoparticle superstructures exhibiting intense chiroptical activity. Merg, A.D., Boatz, J.C., Mandal, A., Zhao, G., Mokashi-Punekar, S., Liu, C., Wang, X., Zhang, P., Van der Wel, P.C.A.*, Rosi, N.L.* . (2016) J. Am. Chem. Soc. 138(41): 13655-13663 (DOI) [ACS Reprint]
Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core. Hoop, C.L., Lin, H.-K., Kar, K., Magyarfalvi, G., Lamley, J., Boatz, J.C., Mandal, A., Lewandowski, J., Wetzel, R., Van der Wel, P.C.A.* (2016) Proc. Natl. Acad. Sci. USA 113(6): 1546-1551 [DOI] [PDF+SI]
2015
Structural changes and pro-apoptotic peroxidase activity of cardiolipin-bound mitochondrial cytochrome c. Mandal, A., Hoop, C.L., DeLucia, M., Kodali, R., Kagan, V., Ahn, J., Van der Wel, P.C.A.* (2015) Biophys. J. 109(9): 1873–1884 (DOI)
2014
Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state NMR. Hoop, C.L., Lin, H.-K., Kar, K., Hou, Z., Poirier, M.A., Wetzel, R., Van der Wel, P.C.A.* (2014) Biochemistry 53(42): 6653-6666 (DOI) (BMRB) [OA-PDF]
Lipid Dynamics and Protein-Lipid Interactions in Integral Membrane Proteins: Insights from Solid-State NMR. Van der Wel, P.C.A.* (2014) eMagRes. 3: 111–118 (DOI) (PDF download) (invited)
How Amyloid Precursor Protein Protects Itself from Cleavage. Lin, H.-K., Van der Wel, P.C.A.* (2014) Structure. 22: 361-362 (DOI) (invited)
D-polyglutamine amyloid recruits L-polyglutamine monomers and kills cells. Kar, K., Arduini, I., Drombosky, K.W., Van der Wel, P.C.A.*, Wetzel, R.* (2014) J Mol Biol. 426(4): 816–29 (DOI)
2013
Spinning-rate encoded chemical shift correlations from rotational resonance solid-state NMR experiments. Li, J., and Van der Wel, P.C.A.* (2013) J. Mag. Reson. 230:117-124 [at journal] [DOI]
β-hairpin-mediated nucleation of polyglutamine amyloid formation.Kar, K., Hoop, C.L., Drombosky, K.W., Baker, M.A., Kodali, R., Arduini, I., Van der Wel, P.C.A., Horne, W.S., and Wetzel, R. (2013) J. Mol. Biol., 425(7):1-45 [DOI]
2012
Serine phosphorylation suppresses huntingtin amyloid accumulation by altering protein aggregation properties. Mishra, R., Hoop, C.L., Kodali, R., Sahoo, B., Van der Wel, P.C.A., and Wetzel, R. (2012) J. Mol. Biol., 424(1-2), p. 1-14 [DOI] [PubMed]
Lipid Dynamics and Protein-Lipid Interactions in 2D Crystals Formed with the β-barrel Integral Membrane Protein VDAC1. Eddy, M.T, Ong, T-C., Clark, L., Teijido, O., Van der Wel, P.C.A., Garces, R., Wagner, G., Rostovtseva, T.K., and Griffin, R.G. (2012) J. Am. Chem. Soc., 134(14):6375–87 [DOI] [PubMed]
Domain swapping and amyloid fibril conformation. Van der Wel, P.C.A. (2012) Prion, 6 (3): 211-216 [at journal] [PubMed] [reprint] [PMC] (invited)
Structural Characterization of the Caveolin Scaffolding Domain in Association with Cholesterol-Rich Membranes. Hoop, C.L.#, Sivanandam, V.N.#, Kodali, R., Srnec, M.N., Van der Wel, P.C.A. (2012) Biochemistry, 51(1):90–9 [DOI] [PubMed] [OA-PDF]
2011
Structural complexity of a composite amyloid fibril. Lewandowski, J.R.#, Van der Wel, P.C.A.#, Rigney, M., Grigorieff, N., and Griffin, R.G. (2011) J. Am. Chem Soc. 133(37):14686-98 [DOI/journal] [PubMed]
Amyloid-like fibrils from a domain-swapping protein feature a parallel, in-register conformation without native-like interactions. Li, j., Hoop, C.L., Kodali, R., Sivanandam, V.N., and Van der Wel, P.C.A.* (2011) J. Biol. Chem. 286 (33): 28988–28995 [journal][PubMed][PMC]
The Aggregation-Enhancing Huntingtin N-terminus is Helical in Amyloid Fibrils Sivanandam, V.N.#, Jayaraman, M.#, Hoop, C.L., Kodali, R., Wetzel, R., and Van der Wel, P.C.A.* (2011) J. Am. Chem. Soc. 133(12): 4558–4566[journal][PubMed][PMC][OA-PDF]
2010
Structural Characterization of GNNQQNY Amyloid Fibrils by Magic Angle Spinning NMRVan der Wel, P.C.A., Lewandowski, J.R., and Griffin, R. G. (2010) Biochemistry 49(44): 9457–9469 [at journal] [PubMed]
Dynamic Nuclear Polarization-Enhanced Solid-State NMR Spectroscopy of GNNQQNY Nanocrystals and Amyloid Fibrils.Debelouchina, G.T., Bayro, M.J., Van der Wel, P.C.A., Caporini, M.A., Barnes, A.B., Rosay, M., Maas, W.E., and Griffin, R. G. (2010) Phys. Chem. Chem. Phys. 12(22): 5911-5919 [PubMed]
Time Averaging of NMR Chemical Shifts in the MLF Peptide in the Solid StateDe Gortari, I, Portella, G., Salvatella, X., Bajaj, V.S.; Van der Wel, P.C.A., Yates, J., Segall, M., Pickard, C., Payne, M., and Vendruscolo, M. (2010) J. Am. Chem. Soc. 132 (17): 5993–6000 [PubMed]
2009
Targeted 13C-13C Distance Measurements in a Microcrystalline Protein via J-Decoupled Rotational Resonance Width Measurements. Van der Wel, P.C.A.; Eddy, M.T.; Ramachandran, R., and Griffin, R.G. (2009) ChemPhysChem 10 (9-10): 1656-1663 [DOI]
High-Resolution Solid-State NMR Structure of Alanyl-Prolyl-Glycine.Barnes, A.B.; Andreas, L.; Huber, M.; Ramachandran, R.; Van der Wel, P.C.A.; Veshtort, M.; Griffin, R.G., and Griffin, R.G. (2009) J. Mag. Res. 200 (1), 95-100 [DOI]
Cryogenic sample exchange NMR probe for magic angle spinning dynamic nuclear polarizationBarnes, A.B.; Mak-Jurkauskas, M.L.; Matsuki, Y.; Bajaj, V.S.; Van der Wel, P.C.A.; DeRocher, R.; Bryant, J.; Sirigiri, J.R.; Temkin, R.J.; Lugtenburg, J.; Herzfeld, J., and Griffin, R.G. (2009) J. Mag. Res. 198 (2): 261-270 [DOI]
Observation of a low-temperature, dynamically driven structural transition in a polypeptide by solid state NMR spectroscopyBajaj, V.S.; Van der Wel, P.C.A., and Griffin, R.G. (2009) J. Am. Chem. Soc. 131(1): 118–128 [Online] [PMC-PDF]
2008
High field dynamic nuclear polarization for solid and solution biological NMR (review article)Barnes, A.B.; De Paëpe, G.; Van der Wel, P.C.A.; Hu, K.-N.; Joo, C.-G.; Bajaj, V.S.; Mak-Jurkauskas, M.L.; Sirigiri, J.R.; Herzfeld, J.; Temkin, R.J., and Griffin, R.G. (2008) Appl. Magn. Reson. 34(3-4): 237-263 [Online] [DOI] [PMC-PDF]
Dynamic nuclear polarization at high magnetic fields(review article)Maly, T.; Debelouchina, G.T.; Bajaj, V.S.; Hu, K.-N.; Joo, C.-G.; Mak-Jurkauskas, M.L.; Sirigiri, J.R.; Van der Wel, P.C.A.; Herzfeld, J.; Temkin, R.J., and Griffin, R.G. (2008) J. Chem. Phys. 128(1): 052211 [DOI] [PMC-PDF]
Helical distortion in tryptophan and lysine anchored membrane-spanning alpha helices as a function of hydrophobic mismatch: A solid-state deuterium NMR investigation using the GALA methodDaily, A.E.; Greathouse, D.V.; Van der Wel, P.C.A., and Koeppe, R.E., II (2008) Biophys. J. 94: 480-491 [DOI] [PMC-PDF]
2007
Solid state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p.Van der Wel, P.C.A.; Lewandowski, J.R., and Griffin, R.G. (2007) J. Am. Chem. Soc. 129(16): 5117-5130 [Online] [DOI]
Orientation and motion of tryptophan interfacial anchors in membrane-spanning peptides.Van der Wel, P.C.A.*; Reed, N.D.; Greathouse, D.V., and Koeppe, R.E., II (2007) Biochemistry 46(25):7514-24 [DOI] [PMC PDF]
2006
Dynamic nuclear polarization of amyloidogenic peptide nanocrystals: GNNQQNY, a core segment of the yeast prion protein Sup35p.Van der Wel, P.C.A.; Hu, K.-N.; Lewandowski, J.R., and Griffin, R.G. (2006) J. Am. Chem. Soc. 128(33):10840-10846 [DOI]
Multipole-multimode Floquet theory of rotational resonance width experiments: 13C-13C distance measurements in uniformly labeled solids.Ramachandran, R.; Lewandowski, J.R.; Van der Wel, P.C.A., and Griffin, R.G. (2006) J. Chem. Phys. 124(21): 214107 Abstract [DOI]
2005
Importance of tensor asymmetry for the analysis of 2H-NMR spectra from deuterated aromatic rings.Pulay, P.; Scherer, E.M.; Van der Wel, P.C.A., and Koeppe, R.E. II (2005) J. Am. Chem. Soc. 127(49): 17488-93. [DOI] [PMC PDF]
2004
Complexes obtained by electrophilic attack on a dinitrogen-derived terminal molybdenum nitride: electronic structure analysis by solid state CP/MAS 15N NMR in combination with DFT calculations.Sceats, E.L.; Figueroa, J.S.; Cummins, C.C.; Loening, N.M.; Van der Wel, P.C.A., and Griffin, R.G. (2004) Polyhedron 23: 2751-2768 [DOI]
Tilt angles of transmembrane model peptides in oriented and nonoriented lipid bilayers as determined by 2H solid-state NMR.Strandberg, E.; Ozdirekcan, S.; Rijkers, D.T.; Van der Wel, P.C.A.; Koeppe, R.E. II; Liskamp, R.M., and Killian, J.A. (2004)Biophys J. 86: 3709-3721 [DOI] [PMC PDF]
2003
Combined experimental/theoretical refinement of indole ring geometry using deuterium magnetic resonance and ab initio calculations.Koeppe, R.E., II; Sun, H.; Van der Wel, P.C.A.; Scherer, E.M.; Pulay, P., and Greathouse, D.V. (2003) J. Am. Chem. Soc. 125: 12268-12276. [DOI]
Hydrophobic mismatch between helices and lipid bilayers.Weiss, T.M.; Van der Wel, P.C.A.; Killian, J.A.; Koeppe, R.E., II, and Huang, H.W. (2003) Biophys J. 84: 379-385 [DOI] [PMC PDF]
2002
Geometry and intrinsic tilt of a tryptophan anchored membrane spanning peptide by 2H NMR.Van der Wel, P.C.A.*; Strandberg, E.; Killian, J.A., and Koeppe, R.E., II (2002) Biophys. J. 83(3): 1479-1488 [DOI] [Info] [PMC PDF]
Lipid dependence of membrane anchoring properties and snorkeling behaviour of aromatic and charged residues in transmembrane peptides. Strandberg, E.; Morein, S.; Rijkers, D.T.S.; Liskamp, R.M.J.; Van der Wel, P.C.A., and Killian, J.A. (2002) Biochemistry 41(23): 7190-7198 [Abstract] [PubMed]
2001
Optimized aminolysis conditions for cleavage of N-protected hydrophobic peptides from solid-phase resins.Greathouse, D.V.; Goforth, R.L.; Crawford, T.; Van der Wel, P.C.A., and Killian, J.A. (2001) J. Peptide Res. 57: 519-527. [Abstract] [PubMed]
2000
Tryptophan-anchored transmembrane peptides promote formation of nonlamellar phases in phosphatidylethanolamine model membranes in a mismatch-dependent manner. Van der Wel, P.C.A.; Pott, T.; Morein, S.; Greathouse, D.V.; Koeppe II, R.E., and Killian, J.A. (2000) Biochemistry 39: 3124-33. [Abstract] [Info] [PDF] [DOI]
<2000
Peptide influences on lipids. Killian, J.A.; Morein, S.; Van der Wel, P.C.A.; De Planque, M.R.R.; Greathouse, D.V., and Koeppe, R.E., II. (1999) Novartis Found Symp. 225: 170-83; discussion 183-7. [Abstract]
Modulation of membrane structure and function by hydrophobic mismatch between proteins and lipids Killian, J.A.; De Planque, M.R.R.; Van der Wel, P.C.A.; Salemink, I.; De Kruijff, B.; Greathouse, D.V., and Koeppe, R.E., II (1998) Pure & Appl. Chem. 70: 75-82. [PDF]