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ResearchZernike (ZIAM)Solid State Nuclear Magnetic ResonanceVan der Wel Group



Structural fingerprinting of protein aggregates by DNP-enhanced solid-state NMR at natural isotopic abundance. Smith, A.N., Marker, K., Piretra, T., Boatz, J.C., Matlahov, I., Kodali, R., Hediger, S., van der Wel, P.C.A., & De Paepe, G. (2018) J. Am. Chem. Soc.,  140(44): 14576-80 [ URL ] [ Full-Text ]

Hidden motions and motion-induced invisibility: dynamics-based spectral editing in solid-state NMR. Matlahov, I., Van der Wel, P.C.A. Methods, in press [ URL ]

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., in press [ 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 ]


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. [ URL ]

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. [ 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 in press [ 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 ]


MAS 1 H 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 )


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 )


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 )


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 ]


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 ] [ Full-text in 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 ]


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 ]


Structural Characterization of GNNQQNY Amyloid Fibrils by Magic Angle Spinning NMR Van 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 State De 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 ]


Targeted 13 C- 13 C 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 polarization Barnes, 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 spectroscopy Bajaj, V.S.; Van der Wel, P.C.A., and Griffin, R.G. (2009) J. Am. Chem. Soc. 131(1): 118–128 [ Online ] [ PMC-PDF ]


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 method Daily, 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 ]


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 [ Abstract ] [ DOI ] [ PMC PDF ]


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 [ Abstract ] [ DOI ]

Multipole-multimode Floquet theory of rotational resonance width experiments: 13 C- 13 C 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 ]


Importance of tensor asymmetry for the analysis of 2 H-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 ]


Complexes obtained by electrophilic attack on a dinitrogen-derived terminal molybdenum nitride: electronic structure analysis by solid state CP/MAS 15 N 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 2 H 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 ]


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. [ Abstract ] [ 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 ]


Geometry and intrinsic tilt of a tryptophan anchored membrane spanning peptide by 2 H 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 ]


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 ]


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 ]


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 ]

Last modified:29 January 2019 10.23 a.m.