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

Publications

2019

Matlahov, I., & van der Wel, P. C. A. (2019). Conformational studies of pathogenic expanded polyglutamine protein deposits from Huntington's disease. Experimental biology and medicine (Maywood, N.J.). https://doi.org/10.1177/1535370219856620
Li, M., Mandal, A., Tyurin, V. A., DeLucia, M., Ahn, J., Kagan, V. E., & van der Wel, P. C. A. (2019). Surface-Binding to Cardiolipin Nanodomains Triggers Cytochrome c Pro-apoptotic Peroxidase Activity via Localized Dynamics. Structure. https://doi.org/10.1016/j.str.2019.02.007

2018

Smith, A. N., Märker, K., Piretra, T., Boatz, J. C., Matlahov, I., Kodali, R. B., ... De Paëpe, G. (2018). Structural fingerprinting of protein aggregates by DNP-enhanced solid-state NMR at natural isotopic abundance. Journal of the American Chemical Society, 140(44), 14576-14580. https://doi.org/10.1021/jacs.8b09002
Matlahov, I., & van der Wel, P. C. A. (2018). Hidden motions and motion-induced invisibility: Dynamics-based spectral editing in solid-state NMR. Methods, 148, 123-135. https://doi.org/10.1016/j.ymeth.2018.04.015
Witkowski, A., Chan, G. K. L., Boatz, J. C., Li, N. J., Inoue, A. P., Wong, J. C., ... Cavigiolio, G. (2018). Methionine oxidized apolipoprotein A-I at the crossroads of HDL biogenesis and amyloid formation. FASEB Journal, 32(6), 3149-3165. https://doi.org/10.1096/fj.201701127R
van der Wel, P. C. A. (2018). New applications of solid-state NMR in structural biology. Emerging topics in life sciences, 2(1), 57-67. https://doi.org/10.1042/ETLS20170088
Boatz, J. C., Chan, G., Witkowski, A., van der Wel, P. C. A., & Cavigiolio, G. (2018). Magic Angle Spinning Solid State NMR Studies of Oxidized Apolipoprotein A-I Aggregates. Biophysical Journal, 114(3), 569A-569A.
Li, M., Mandal, A., DeLucia, M., Ahn, J., Tyurin, V. A., Kagan, V. E., & van der Wel, P. C. A. (2018). Structural Plasticity of the Pivotal Cytochrome C/Cardiolipin Complex in Mitochondrial Apoptosis. Biophysical Journal, 114(3), 198A-198A. https://doi.org/10.1016/j.bpj.2017.11.1108

2017

Periole, X., Huber, T., Bonito-Oliva, A., Aberg, K. C., van der Wel, P. C. A., Sakmar, T. P., & Marrink, S. J. (2018). Energetics Underlying Twist Polymorphisms in Amyloid Fibrils. The Journal of Physical Chemistry. B: Materials, Surfaces, Interfaces, & Biophysical, 122(3), 1081–1091. https://doi.org/10.1021/acs.jpcb.7b10233
van der Wel, P. C. A. (2017). Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy. Solid state nuclear magnetic resonance, 88, 1-14. https://doi.org/10.1016/j.ssnmr.2017.10.001
Lin, H-K., Boatz, J. C., Krabbendam, I. E., Kodali, R., Hou, Z., Wetzel, R., ... van der Wel, P. C. A. (2017). Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core. Nature Communications, 8, [15462]. https://doi.org/10.1038/ncomms15462
Boatz, J. C., Whitley, M. J., Li, M., Gronenborn, A. M., & van der Wel, P. C. A. (2017). Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH. Nature Communications, 8, 15137. https://doi.org/10.1038/ncomms15137
Mandal, A., Boatz, J. C., Wheeler, T. B., & van der Wel, P. C. A. (2017). On the use of ultracentrifugal devices for routine sample preparation in biomolecular magic-angle-spinning NMR. Journal of Biomolecular Nmr, 67(3), 165-178. https://doi.org/10.1007/s10858-017-0089-6
Kar, K., Baker, M. A., Lengyel, G. A., Hoop, C. L., Kodali, R., Byeon, I-J., ... Wetzel, R. (2017). Backbone Engineering within a Latent β-Hairpin Structure to Design Inhibitors of Polyglutamine Amyloid Formation. Journal of Molecular Biology, 429(2), 308-323. https://doi.org/10.1016/j.jmb.2016.12.010

2016

Mandal, A., & van der Wel, P. C. A. (2016). MAS H NMR Probes Freezing Point Depression of Water and Liquid-Gel Phase Transitions in Liposomes. Biophysical Journal, 111(9), 1965-1973. https://doi.org/10.1016/j.bpj.2016.09.027
Merg, A. D., Boatz, J. C., Mandal, A., Zhao, G., Mokashi-Punekar, S., Liu, C., ... Rosi, N. L. (2016). Peptide-Directed Assembly of Single-Helical Gold Nanoparticle Superstructures Exhibiting Intense Chiroptical Activity. Journal of the American Chemical Society, 138(41), 13655-13663. https://doi.org/10.1021/jacs.6b07322
Merg, A., Zhao, G., Mandal, A., Boatz, J., Wang, X., Van der Wel, P., ... Rosi, N. (2016). Peptide-directed synthesis of single helical gold nanoparticle superstructures. Abstracts of Papers of the American Chemical Society, 252.
Boatz, J. C., Whitley, M. J., Hoop, C. L., Zeng, X., Yates, N., Gronenborn, A. M., & van der Wel, P. C. A. (2016). An Investigation of the Atomic Structure of Cataract-Forming Mutant Gamma-D-Crystallin Aggregates Formed under Distinct Environmental Conditions. Biophysical Journal, 110(3), 27A-27A. https://doi.org/10.1016/j.bpj.2015.11.210
Mandal, A., Hoop, C. L., Kodali, R., Di, M., DeLucia, M., Kagan, V. E., ... van der Wel, P. C. A. (2016). To Unfold or not to Unfold? Structural Insights of Peroxidase-Active Cardiolipin-Bound Cytochrome c by Solid-State NMR. Biophysical Journal, 110(3), 577A-578A. https://doi.org/10.1016/j.bpj.2015.11.3088
Hoop, C. L., Lin, H. K., Kar, K., Magyarfalvi, G., Lamley, J. M., Boatz, J. C., ... Van Der Wel, P. C. A. (2016). Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core. Proceedings of the National Academy of Sciences of the United States of America, 113(6), 1546-1551. https://doi.org/10.1073/pnas.1521933113

2015

Mandal, A., Hoop, C. L., DeLucia, M., Kodali, R., Kagan, V. E., Ahn, J., & van der Wel, P. C. A. (2015). Structural Changes and Proapoptotic Peroxidase Activity of Cardiolipin-Bound Mitochondrial Cytochrome c. Biophysical Journal, 109(9), 1873-84. https://doi.org/10.1016/j.bpj.2015.09.016
van der Wel, P. (2015). Nuclear Magnetic Resonance Studies of Polyglutamine's Misfolded Conformation in the Aggregated State. FASEB Journal, 29.
Hoop, C. L., Lin, H-K., Kar, K., Wetzel, R., & van der Wel, P. C. A. (2015). Huntingtin N-Terminal Fragment Fibrils have a Rigid Amyloid Core Flanked by Non-Amyloid Domains with Increased Dynamics. Biophysical Journal, 108(2), 385A-386A. https://doi.org/10.1016/j.bpj.2014.11.2114

2014

Hoop, C. L., Lin, H-K., Kar, K., Hou, Z., Poirier, M. A., Wetzel, R., & van der Wel, P. C. A. (2014). Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance. Biochemistry, 53(42), 6653-66. https://doi.org/10.1021/bi501010q
van der Wel, P. C. A. (2014). Lipid Dynamics and Protein-Lipid Interactions in Integral Membrane Proteins: Insights from Solid-State NMR. In R. K. Harris, & R. L. Wasylishen (Eds.), eMagRes (pp. 111-118). John Wiley & Sons. https://doi.org/10.1002/9780470034590.emrstm1356
Lin, H-K., & van der Wel, P. C. A. (2014). How amyloid precursor protein protects itself from cleavage. Structure, 22(3), 361-362. https://doi.org/10.1016/j.str.2014.02.008
Kar, K., Arduini, I., Drombosky, K. W., van der Wel, P. C. A., & Wetzel, R. (2014). D-polyglutamine amyloid recruits L-polyglutamine monomers and kills cells. Journal of Molecular Biology, 426(4), 816-829. https://doi.org/10.1016/j.jmb.2013.11.019

2013

Li, J., & van der Wel, P. C. A. (2013). Spinning-rate encoded chemical shift correlations from rotational resonance solid-state NMR experiments. Journal of Magnetic Resonance, 230, 117-24. https://doi.org/10.1016/j.jmr.2013.02.004
Kar, K., Hoop, C. L., Drombosky, K. W., Baker, M. A., Kodali, R., Arduini, I., ... Wetzel, R. (2013). β-hairpin-mediated nucleation of polyglutamine amyloid formation. Journal of Molecular Biology, 425(7), 1183-1197. https://doi.org/10.1016/j.jmb.2013.01.016
Hoop, C. L., Mishra, R., Kar, K., Kodali, R., Wetzel, R., & van der Wel, P. C. A. (2013). Structural and Motional Investigations of Polyglutamine-Containing Amyloid Fibrils by Magic-Angle-Spinning Solid-State NMR. Biophysical Journal, 104(2), 181A-181A. https://doi.org/10.1016/j.bpj.2012.11.1017
Hoop, C. L., Sivanandam, V. N., Srnec, M. N., Kodali, R., & van der Wel, P. C. A. (2013). Structural Studies of a Membrane-Bound Cholesterol Recognition Motif by Solid-State NMR. Biophysical Journal, 104(2), 97A-97A. https://doi.org/10.1016/j.bpj.2012.11.574

2012

Mishra, R., Hoop, C. L., Kodali, R., Sahoo, B., van der Wel, P. C. A., & Wetzel, R. (2012). Serine phosphorylation suppresses huntingtin amyloid accumulation by altering protein aggregation properties. Journal of Molecular Biology, 424(1-2), 1-14. https://doi.org/10.1016/j.jmb.2012.09.011
van der Wel, P. C. A. (2012). Domain swapping and amyloid fibril conformation. Prion, 6(3), 211-6. https://doi.org/10.4161/pri.18987
Eddy, M. T., Ong, T-C., Clark, L., Teijido, O., van der Wel, P. C. A., Garces, R., ... Griffin, R. G. (2012). Lipid dynamics and protein-lipid interactions in 2D crystals formed with the β-barrel integral membrane protein VDAC1. Journal of the American Chemical Society, 134(14), 6375-6387. https://doi.org/10.1021/ja300347v
Hoop, C. L., Sivanandam, V. N., Kodali, R., Srnec, M. N., & van der Wel, P. C. A. (2012). Structural characterization of the caveolin scaffolding domain in association with cholesterol-rich membranes. Biochemistry, 51(1), 90-99. https://doi.org/10.1021/bi201356v

2011

Lewandowski, J. R., van der Wel, P. C. A., Rigney, M., Grigorieff, N., & Griffin, R. G. (2011). Structural complexity of a composite amyloid fibril. Journal of the American Chemical Society, 133(37), 14686-1498. https://doi.org/10.1021/ja203736z
Li, J., Hoop, C. L., Kodali, R., Sivanandam, V. N., & van der Wel, P. C. A. (2011). Amyloid-like fibrils from a domain-swapping protein feature a parallel, in-register conformation without native-like interactions. The Journal of Biological Chemistry, 286(33), 28988-28995. https://doi.org/10.1074/jbc.M111.261750
Sivanandam, V. N., Jayaraman, M., Hoop, C. L., Kodali, R., Wetzel, R., & van der Wel, P. C. A. (2011). The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils. Journal of the American Chemical Society, 133(12), 4558-4566. https://doi.org/10.1021/ja110715f

2010

van der Wel, P. C. A., Lewandowski, J. R., & Griffin, R. G. (2010). Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMR. Biochemistry, 49(44), 9457-69. https://doi.org/10.1021/bi100077x
Debelouchina, G. T., Bayro, M. J., van der Wel, P. C. A., Caporini, M. A., Barnes, A. B., Rosay, M., ... Griffin, R. G. (2010). Dynamic nuclear polarization-enhanced solid-state NMR spectroscopy of GNNQQNY nanocrystals and amyloid fibrils. PPCP : Physical Chemistry Chemical Physics, 12(22), 5911-5919. https://doi.org/10.1039/c003661g
De Gortari, I., Portella, G., Salvatella, X., Bajaj, V. S., van der Wel, P. C. A., Yates, J. R., ... Vendruscolo, M. (2010). Time averaging of NMR chemical shifts in the MLF peptide in the solid state. Journal of the American Chemical Society, 132(17), 5993-6000. https://doi.org/10.1021/ja9062629

2009

Barnes, A. B., Andreas, L. B., Huber, M., Ramachandran, R., van der Wel, P. C. A., Veshtort, M., ... Mehta, M. A. (2009). High-resolution solid-state NMR structure of alanyl-prolyl-glycine. Journal of Magnetic Resonance, 200(1), 95-100. https://doi.org/10.1016/j.jmr.2009.06.009
van der Wel, P. C. A., Eddy, M. T., Ramachandran, R., & Griffin, R. G. (2009). Targeted 13C-13C distance measurements in a microcrystalline protein via J-decoupled rotational resonance width measurements. Chemphyschem, 10(9-10), 1656-1663. https://doi.org/10.1002/cphc.200900102
Barnes, A. B., Mak-Jurkauskas, M. L., Matsuki, Y., Bajaj, V. S., van der Wel, P. C. A., Derocher, R., ... Griffin, R. G. (2009). Cryogenic sample exchange NMR probe for magic angle spinning dynamic nuclear polarization. Journal of Magnetic Resonance, 198(2), 261-270. https://doi.org/10.1016/j.jmr.2009.03.003
Eddy, M., Garces, R., van der Wel, P. C. A., Wagner, G., & Griffin, R. (2009). Magic Angle Spinning NMR Investigations of the Human Voltage Dependent Anion Channel. Biophysical Journal, 96(3), 410A-410A. https://doi.org/10.1016/j.bpj.2008.12.2090
van der Wel, P. C. A., Lewandowski, J. R., & Griffin, R. G. (2009). Solid State NMR Studies Of Structural And Motional Complexity In Amyloid-Like Fibrils Of The Peptide GNNQQNY. Biophysical Journal, 96(3), 219A-219A.
Bajaj, V. S., van der Wel, P. C. A., & Griffin, R. G. (2009). Observation of a low-temperature, dynamically driven structural transition in a polypeptide by solid-state NMR spectroscopy. Journal of the American Chemical Society, 131(1), 118-128. https://doi.org/10.1021/ja8045926

2008

Barnes, A. B., De Paëpe, G., van der Wel, P. C. A., Hu, K-N., Joo, C-G., Bajaj, V. S., ... Griffin, R. G. (2008). High-Field Dynamic Nuclear Polarization for Solid and Solution Biological NMR. Applied magnetic resonance, 34(3-4), 237-263. https://doi.org/10.1007/s00723-008-0129-1
Maly, T., Debelouchina, G. T., Bajaj, V. S., Hu, K-N., Joo, C-G., Mak-Jurkauskas, M. L., ... Griffin, R. G. (2008). Dynamic nuclear polarization at high magnetic fields. The Journal of Chemical Physics, 128(5), 052211-1 - 052211-19. [052211]. https://doi.org/10.1063/1.2833582
Daily, A. E., Greathouse, D. V., van der Wel, P. C. A., & Koeppe, R. E. (2008). 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 geometric analysis of labeled alanines method. Biophysical Journal, 94(2), 480-491. https://doi.org/10.1529/biophysj.106.097543

2007

van der Wel, P. C. A., Reed, N. D., Greathouse, D. V., & Koeppe, R. E. (2007). Orientation and motion of tryptophan interfacial anchors in membrane-spanning peptides. Biochemistry, 46(25), 7514-7524. https://doi.org/10.1021/bi700082v
van der Wel, P. C. A., Lewandowski, J. R., & Griffin, R. G. (2007). Solid-state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p. Journal of the American Chemical Society, 129(16), 5117-5130. https://doi.org/10.1021/ja068633m
van der Wel, P. C. A., Lewandowski, J. R., & Griffin, R. G. (2007). Features of crystal and fibril formation by GNNQQNY, peptide fragment of yeast prion protein sup35p. Biophysical Journal, 195A-195A.
Daily, A. E., Greathouse, D. V., van der Wel, P. C. A., & Koeppe, R. E. (2007). Intrinsic kinking of transmembrane alpha-helical peptides as a function of hydrophobic mismatch. Biophysical Journal, 70A-70A.

2006

van der Wel, P. C. A., Hu, K-N., Lewandowski, J., & Griffin, R. G. (2006). Dynamic nuclear polarization of amyloidogenic peptide nanocrystals: GNNQQNY, a core segment of the yeast prion protein Sup35p. Journal of the American Chemical Society, 128(33), 10840-10846. https://doi.org/10.1021/ja0626685
Ramachandran, R., Lewandowski, J. R., van der Wel, P. C. A., & Griffin, R. G. (2006). Multipole-multimode Floquet theory of rotational resonance width experiments: 13C-13C distance measurements in uniformly labeled solids. The Journal of Chemical Physics, 124(21), 214107-1 - 214107-13. [214107]. https://doi.org/10.1063/1.2194905

2005

Pulay, P., Scherer, E. M., van der Wel, P. C. A., & Koeppe, R. E. (2005). Importance of tensor asymmetry for the analysis of 2H NMR spectra from deuterated aromatic rings. Journal of the American Chemical Society, 127(49), 17488-17493. https://doi.org/10.1021/ja054935x

2004

Strandberg, E., Ozdirekcan, S., Rijkers, D. T. S., van der Wel, P. C. A., Koeppe, R. E., Liskamp, R. M. J., & Killian, J. A. (2004). Tilt angles of transmembrane model peptides in oriented and non-oriented lipid bilayers as determined by 2H solid-state NMR. Biophysical Journal, 86(6), 3709-3721. https://doi.org/10.1529/biophysj.103.035402

2003

Weiss, T. M., van der Wel, P. C. A., Killian, J. A., Koeppe, R. E., & Huang, H. W. (2003). Hydrophobic mismatch between helices and lipid bilayers. Biophysical Journal, 84(1), 379-385. https://doi.org/10.1016/S0006-3495(03)74858-9
Koeppe, R. E., Sun, H., van der Wel, P. C. A., Scherer, E. M., Pulay, P., & Greathouse, D. V. (2003). Combined experimental/theoretical refinement of indole ring geometry using deuterium magnetic resonance and ab initio calculations. Journal of the American Chemical Society, 125(40), 12268-12276. https://doi.org/10.1021/ja035052d

2002

van der Wel, P. C. A., Strandberg, E., Killian, J. A., & Koeppe, R. E. (2002). Geometry and intrinsic tilt of a tryptophan-anchored transmembrane alpha-helix determined by (2)H NMR. Biophysical Journal, 83(3), 1479-1488. https://doi.org/10.1016/S0006-3495(02)73918-0
Strandberg, E., Morein, S., Rijkers, D. T. S., Liskamp, R. M. J., van der Wel, P. C. A., & Killian, J. A. (2002). Lipid dependence of membrane anchoring properties and snorkeling behavior of aromatic and charged residues in transmembrane peptides. Biochemistry, 41(23), 7190-7198. https://doi.org/10.1021/bi012047i

2001

Greathouse, D. V., Goforth, R. L., Crawford, T., Van Der Wel, P. C. A., & Killian, J. A. (2001). Optimized aminolysis conditions for cleavage of N-protected hydrophobic peptides from solid-phase resins. The journal of peptide research : official journal of the American Peptide Society, 57(6), 519-527. https://doi.org/10.1034/j.1399-3011.2001.00849.x

2000

van der Wel, P. C., Pott, T., Morein, S., Greathouse, D. V., Koeppe, R. E., & Killian, J. A. (2000). Tryptophan-anchored transmembrane peptides promote formation of nonlamellar phases in phosphatidylethanolamine model membranes in a mismatch-dependent manner. Biochemistry, 39(11), 3124-3133.

1999

Killian, J. A., Morein, S., van der Wel, P. C., de Planque, M. R., Greathouse, D. V., & Koeppe, R. E. (1999). Peptide influences on lipids. Novartis Foundation symposium, 225, 170-83; discussion 183-7.

Publications before moving to RUG:

2018

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 ]

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. [ 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 ]

2016

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 )

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 ] [ 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 ]

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 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 ]

2009

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 ]

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 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 ]

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 [ Abstract ] [ 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 [ 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 ]

2005

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 ]

2004

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 ]

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. [ 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 ]

2002

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 ]

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 ]

Last modified:04 June 2019 12.16 p.m.