Publications
Vugmeyster L., Fu R., Ostrovsky D., 17O NMR relaxation measurements for investigation of molecular dynamics in static solids, using sodium nitrate as a model compound. Solid State Nucl. Magn. Reson. 2024, submitted.SSNR: https://ssrn.com/abstract=4944103
Biedenbänder T, Rodgers A, Schröder M, Vugmeyster L. Björn Corzilius B. Investigation of biomolecular dynamics by sensitivity-enhanced 1H-2H CPMAS NMR usingmatrix-free dynamic nuclear polarization, J. Magn. Reason. Open Access, 2024 in press, https://doi.org/10.1016/j.jmro.2024.100161
Vugmeyster L, Ostrovsky D, Fu R. (2024) Solid State NMR 130, 101922 (2024) Carbon-detected deuterium solid-state NMR rotating frame relaxation measurements for protein methyl groups under magic angle spinning
Vugmeyster L, Au DF, Frazier B, Qiang W, Ostrovsky D, Phys. Chem. Chem. Phys. 26, 5466 - 5478 (2024) Rigidifying of the internal dynamics of amyloid-beta fibrils generated in the presence of synaptic plasma vesicles
Vugmeyster L, Ostrovsky D, Rodgers A, Gwin K, Smirnov SL, McKnight CJ, Fu R, (2024) ChemPhysChem. 25, e202300565, Persistence of Methionine Side Chain Mobility at Low Temperatures in a Nine-Residue Low Complexity Peptide, as Probed by 2H Solid-State NMR
Cruceta, L; Sun Y., Kenyaga JM, Ostrovsky D, Rodgers A., Vugmeyster L., Yao L., Qiang W. (2023) J. Biol. Chem. 299, 105196. IModulation of aggregation and structural polymorphisms of β-amyloid fibrils in cellular environments by pyroglutamate-3 variant cross-seeding
Vugmeyster L, Rodgers A, Ostrovsky D, McKnight, CJ, Fu R. (2023) J. Magn. Reson. 352. 107493. Deuteron off-resonance rotating frame relaxation for the characterization of slow motions in rotating and static solid-state proteins
Rodgers A, Sawaged M, Ostrovsky D, Vugmeyster L (2023) J. Phys. Chem. B 127, 13, 2887–2899 Effect of Cross-seeding of Wild-type Amyloid-β1-40 Peptide with Post-translationally Modified Fibrils on Internal Dynamics of the Fibrils Using Deuterium Solid-state NMR.
Vugmeyster L, Nichol PJ, Ostrovsky D, Mcknight CJ, Vogeli B (2023) Magnetochemistry, 9, 33.. Slow Methyl Axes Motions in Perdeuterated Villin Headpiece Subdomain Probed by Cross-Correlated NMR Relaxation Measurements
Vugmeyster L, Ostrovsky D, Greenwood A, Fu R. (2022) J. Magn. Reson. 337, 107171. Deuteron rotating frame relaxation for the detection of slow motions in rotating solids
Vugmeyster L, Au DF, Smith MC, Ostrovsky D (2022) ChemPhysChem 2022, 23, e202100709. Comparative Hydrophobic Core Dynamics Between Wild-Type Amyloid-β Fibrils, Glutamate-3 Truncation, and Serine-8 Phosphorylation
Vugmeyster L, Ostrovsky D, Greenwood A, Fu R. Front. Mol. Biosci. (2021), 8. Deuteron Chemical Exchange Saturation Transfer for the Detection of Slow Motions in Rotating Solids
Vugmeyster, L. (2021) Solid State Nucl. Magn. Reson, 11, 101710 . Recent Developments in Deuterium Solid-State NMR for the Detection of Slow Motions in Proteins
Vugmeyster L, Ostrovsky D (2020) Magn Reson Chem. (9-10), 853-863. Deuterium Solid-State NMR Quadrupolar Order Rotating Frame Method with Applications to Amyloid-β Fibrils
Vugmeyster L, Au DF, Ostrovsky D, Rickertsen D, Reed S (2020) J Phys Chem B 124, 23, 4723–4731 Dynamics of Serine-8 Side-Chain in Amyloid-β Fibrils and Fluorenylmethyloxycarbonyl Serine Amino Acid, Investigated by Solid-State Deuteron NMR
Hu Z, Au DF, Cruceta L, Vugmeyster L, Qiang W (2020) ACS Chem Neurosci 11, 14, 2058–2065 The N-Terminal Modified Aβ Variants Enable Modulations to the Structures and Cytotoxicity Levels of Wild-Type Aβ Fibrils through Cross-Seeding
Nichols PJ, Falconer IB, Griffin A, Mant C. Hodges R, McKnight CJ, Vögeli B, Vugmeyster L (2020) Prot Sci 29, 1641-1654 Deuteration of Non-Exchangeable Protons on Proteins Affects Their Thermal Stability, Side-Chain Dynamics and Hydrophobicity.
Vugmeyster L, Ostrovsky D,, Fu R, Chemphyschem. (2020) 21(3):220-231 Deuteron Quadrupolar Chemical Exchange Saturation Transfer (Q‐CEST) Solid‐State NMR for Static Powder Samples: Approach and Applications to Amyloid‐β Fibrils
Vugmeyster L, Au, DF, Ostrovsky D, Kierl B, Fu R, Hu Z, Qiang W Biophys J 117, 1524-1535 (2019) Effect of Post-Translational Modifications and Mutations on Amyloid-β Fibrils Dynamics at N-Terminus
Hu Z, Vugmeyster L , Ostrovsky D, Au DF, Sun Y, Qiang W PNAS (2019) 116 (23) 11253-11258 Molecular structure of an N-terminal phosphorylated β-amyloid fibril
Au DF, Ostrovsky D, Fu R, Vugmeyster L. J Biol Chem 294, 5840-5853. (2019) Solid-state NMR reveals a comprehensive view of the dynamics of the flexible, disordered N-terminal domain of amyloid-β fibrils
Vugmeyster L, Ostrovsky D, Fu R ChemPhysChem 20, 1680-1689. ( 2019) Deuteron Solid‐State NMR Relaxation Measurements Reveal Two Distinct Conformational Exchange Processes in the Disordered N‐Terminal Domain of Amyloid‐β Fibrils
Vugmeyster L, Griffin A, Ostrovsky D, Bhattacharya S, Nichols PJ, McKnight CJ, Vögeli B.J Biomol NMR. 72, 39054 (2018) Correlated motions of C'-N and Cα-Cβ pairs in protonated and per-deuterated GB3
Vögeli B, Vugmeyster L. Chemphyschem. 20, 178-196 ( 2019) Distance-independent Cross-correlated Relaxation and Isotropic Chemical Shift Modulation in Protein Dynamics Studies
Vugmeyster L, Ostrovsky D. Chemphyschem. 20, 333-342 (2019) Deuterium Rotating Frame NMR Relaxation Measurements in the Solid State under Static Conditions for Quantification of Dynamics
Vugmeyster L, Ostrovsky D Methods 148:136-145 (2018) Basic Experiments in 2H static NMR for the Characterization of Protein Side-Chain Dynamics
Miears HL, Gruber DR, Horvath NM, Antos JM, Young J, Sigurjonsson JP, Klem ML, Rosenkranz EA, Okon M, McKnight CJ, Vugmeyster L, Smirnov SL Biochemistry 57, 1690-1701 (2018) Plant Villin Headpiece Domain Demonstrates a Novel Surface Charge Pattern and High Affinity for F-Actin
Falconer IB, Mant CT, McKnight CJ, Vugmeyster L, Hodges R J Chromatography A 1521, 44-52. (2017) Optimized Purification of a Fusion Protein by Reversed-phase High Performance Liquid Chromatography Informed by the Linear Solvent Strength Model
Vugmeyster L, Ostrovsky D, Hoatson GL., Qiang W. Falconer IB J Phys Chem B 121: 7267–7275 (2017) Solvent-Driven Dynamical Crossover in the Phenylalanine Side-Chain from the Hydrophobic Core of Amyloid Fibrils Detected by 2H NMR Relaxation
Vugmeyster L., Hagedorn B, Clark AM, Sletten RS Geoderma 299:25-31 (2017) Evaluating the Effect of Grain Size and Salts on Liquid Water Content in Frozen Soils of Antarctica by Combining NMR, Chemical Equilibrium Modeling, and Scattered Diffraction Analysis.
Vugmeyster L, Ostrovsky D In Press Prog. Nucl. Magn. Reson. Spec., 101:1-17 (2017) Static Solid-state 2H NMR Methods in Studies of Protein Side-chain Dynamics
Vugmeyster L, Ostrovsky D "Chem. Phys. Lett. 67:108-112 (2017)"Comparative Dynamics of Methionine Side-Chain in FMOC-Methionine and in Amyloid Fibrils "
Vugmeyster L, Clark AM, Falconer IB, Ostrovsky D, Hoatson L, Qiang, W, Biophys. J. 111, 2135-2148 (2016) “Fast Motions of Key Methyl Groups in Amyloid-b fibrils”
Vugmeyster L, Clark AM, Falconer IB, Ostrovsky D, Qiang W, Hoatson GL, J. Biol. Chem. 291:18484-95 (2016), “Flexibility and Solvation of Amyloid -b Hydrophobic Core”
Harpole KW, O'Brien ES, Clark, MA, McKnight CJ, Vugmeyster L, Wand A J, Prot. Sci.,25, 423-432 (2016) ” The Unusual Internal Motion of the Villin Headpiece Subdomain”
Vugmeyster L, Ostrovsky D, Villafrance TR, Sharp J, Xu W, Lipton, AS, Hoatson GL, Vold RL, J. Phys. Chem. B, 119, 14892–14904 (2015) “Dynamics of Hydrophobic Core Phenylalanine Residues Probed by Solid-State Deuteron NMR”
Vugmeyster L, Ostrovsky D, Fu R, J. Magn. Reson. 259, 225-231 (2015) ”15N CSA Tensors and 15N-1H Dipolar Couplings of Protein Hydrophobic Core Residues Investigated by Static Solid-State NMR”
Vugmeyster L, Ostrovsky D, J. Chem. Phys., 140, 075101 (2014) “Restricted Diffusion of Methyl Groups in Proteins Revealed by Deuteron NMR: Manifestation of Intra-well Dynamics”
Vugmeyster L, Do T, Ostrovsky D, Fu R, Protein Science 23, 145-156 (2014) “Effect of Subdomain Interactions on Methyl Group Dynamics in the Hydrophobic Core of Villin Headpiece Protein”
Vugmeyster L, Ostrovsky D, Lipton AS J. Phys. Chem. B 117 (20), 6129–6137 (2013) “Origin of Abrupt Rise in Deuteron NMR Longitudinal Relaxation Times of Protein Methyl Groups Below 90 K”
Vugmeyster L, Ostrovsky D, Penland K, Hoatson GL, Vold RL, J. Phys. Chem. B, 117 (4), 1051–1061 (2013) "Glassy Dynamics of Protein Methyl Groups Revealed by Deuteron NMR"
Vugmeyster L, Do T, Ostrovsky D, Fu R, Hagedorn B, Solid State NMR, 45-46, 11-15 (2012) “Characterization of Water Dynamics in Frozen Soils by Solid-State Deuteron NMR”
Vugmeyster L, Ostrovsky D, Khadjinova A, Ellden J, Hoatson GL, Vold RL, Biochemistry, 50, 10637–10646(2011) “Slow Motions in The Hydrophobic Core of Chicken Villin Headpiece Subdomain and their Contributions to Configurational Entropy and Heat Capacity from Solid-State Deuteron NMR measurements”
Vugmeyster L, Ostrovsky D, J. Biomol. NMR, 50(2), 119-127 (2011) “Temperature Dependence of Fast Carbonyl Backbone Dynamics in Chicken Villin Headpiece Subdomain”
Vugmeyster L, Ostrovsky D, Moses M, Ford JJ, Lipton AS, Hoatson GL, Vold RL, J. Phys. Chem. B 114 (48), 15799–15807 (2010) “Comparative dynamics of leucine methyl groups in FMOC-leucine and in a protein hydrophobic core probed by solid-state deuteron NMR over 7-324K temperature range.”
Vugmeyster L, Ostrovsky D, Li, Y, J. Biomol. NMR 47 (2), 155-162 (2010) “Comparison of fast backbone dynamics at amide nitrogen and carbonyl sites in dematin headpiece C-terminal domain and Its S74E mutant”
Vugmeyster L, Ostrovsky D, Ford JJ, Lipton AS, J. Am. Chem. Soc. 132 (12), 4038–4039 (2010) “Freezing of dynamics of a methyl group in a protein hydrophobic core at cryogenic temperatures by deuteron NMR spectroscopy.”
Vugmeyster L, Ostrovsky D, Ford JJ, Burton SD, Lipton AS, Hoatson GL, Vold RL, J. Am. Chem. Soc. 131 (38), 13651–13658 (2009) “Probing the dynamics of a protein hydrophobic core by deuteron solid-state nuclear magnetic resonance spectroscopy.”
Vold RL, Hoatson GL, Vugmeyster L, Ostrovsky D, DeCasto PJ, Phys. Chem. Chem. Phys. 11, 7008-7012 (2009) “Solid state deuteron relaxation time anisotropy measured with multiple echo acquisition.“
Vugmeyster L, Magn. Reson. Chem. 47, 746-751 (2009) “Slow backbone dynamics of chicken villin headpiece subdomain probed by NMR C′-N cross-correlated relaxation.“
Vugmeyster, L, McKnight CJ, J. Biomol. NMR 43, 39-50 (2009). “Phosphorylation-induced changes in backbone dynamics of dematin headpiece C-terminal domain.“
Vugmeyster L, McKnight CJ, Biophys. J. 95, 5941-5960 (2008) “Slow motions in chicken villin headpiece subdomain probed by cross-correlated NMR relaxation of amide NH bonds in successive residues.“
Vugmeyster L, Bodenhausen G, Appl. Magn. Reson., 22, 147-163 (2005) “Temperature-dependent protein backbone dynamics from auto- and cross-correlated NMR relaxation rates.“
Vugmeyster L, Perazzolo C, Wist J, Frueh D, Bodenhausen G, J. Biomol. NMR 28 (2), 173-177 (2004) “Evidence of slow motions by cross-correlated chemical shift modulation in deuterated and protonated proteins.“
Vugmeyster L, Pelupessy P, Vugmeister BE, Abergel D, Bodenhausen G, Comptes Rendus de l'Académie des Sciences (section de Physique) 5 (3), 377-386 (2004) “Cross-correlated relaxation in NMR of macromolecules in the presence of fast and slow dynamics.“
Vugmeyster L, Raleigh DP, Palmer AG, Vugmeister BE, J. Am. Chem. Soc. 125 (27), 8400-8404 (2003) “Beyond the decoupling approximation in the model free approach for the interpretation of NMR relaxation of macromolecules in solution.”
Wang M, Tang Y, Sato S, Vugmeyster L, McKnight CJ, Raleigh DP, J. Am. Chem. Soc. 125 (20), 6032-6033 (2003) "Dynamic NMR lineshape analysis demonstrates that the Villin Headpiece Domain folds on the microsecond time scale."
Vugmeyster L, Trott O, McKnight CJ, Raleigh DP, Palmer AG, J. Mol. Biol., 320 (4), 841-854 (2002) “Temperature-dependent dynamics of the villin headpiece helical subdomain, an unusually small thermostable protein.”
Vugmeyster L, Kroenke CD, Picart F, Palmer AG, Raleigh DP, J. Am. Chem. Soc. 122 (22), 5387-5388 (2000) “N15 R1rho measurements allow the determination of ultrafast protein folding rates.“
Vugmeyster L, Kuhlman B, Raleigh DP, Protein Science, 7 (9), 1994-1997 (1998) "Amide proton exchange measurements as a probe of the stability and dynamics of the N-terminal domain of the ribosomal protein L9: Comparison with the intact protein."