L. Vugmeyster

发表

Flexibility and Solvation of Amyloid-β Hydrophobic Core*

D. Ostrovsky, D. Gantz, G. Hoatson, 2016, The Journal of Biological Chemistry.

Evidence of Slow Motions by Cross-Correlated Chemical Shift Modulation in Deuterated and Protonated Proteins

G. Bodenhausen, D. Frueh, J. Wist, 2004, Journal of biomolecular NMR.

The unusual internal motion of the villin headpiece subdomain

A. Wand, Kyle W. Harpole, C. McKnight, 2016, Protein science : a publication of the Protein Society.

Solid-state NMR reveals a comprehensive view of the dynamics of the flexible, disordered N-terminal domain of amyloid-β fibrils

D. Ostrovsky, R. Fu, L. Vugmeyster, 2019, The Journal of Biological Chemistry.

Characterization of water dynamics in frozen soils by solid-state deuteron NMR.

D. Ostrovsky, R. Fu, B. Hagedorn, 2012, Solid state nuclear magnetic resonance.

Molecular structure of an N-terminal phosphorylated β-amyloid fibril

D. Ostrovsky, Yan Sun, W. Qiang, 2019, Proceedings of the National Academy of Sciences.

Temperature-dependent protein backbone dynamics from auto- and cross-correlated NMR relaxation rates

G. Bodenhausen, L. Vugmeyster, 2005 .

P. Pelupessy, G. Bodenhausen, D. Abergel, 2004 .

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

R. Sletten, B. Hagedorn, M. Clark, 2017 .

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.

D. Ostrovsky, G. Hoatson, R. Vold, 2011, Biochemistry.

Running title : Flexibility and Solvation of A β Hydrophobic Core

D. Ostrovsky, D. Gantz, G. Hoatson, 2016 .

Solid-state NMR reveals a comprehensive view of the dynamics of the flexible, disordered N-terminal domain of amyloid- (cid:2) fibrils

D. Ostrovsky, R. Fu, L. Vugmeyster, 2020 .

Effect of subdomain interactions on methyl group dynamics in the hydrophobic core of villin headpiece protein

D. Ostrovsky, L. Vugmeyster, Tien Do, 2014, Protein science : a publication of the Protein Society.

Phosphorylation-induced changes in backbone dynamics of the dematin headpiece C-terminal domain

C. McKnight, L. Vugmeyster, 2009, Journal of biomolecular NMR.

Static solid-state 2H NMR methods in studies of protein side-chain dynamics.

D. Ostrovsky, L. Vugmeyster, 2017, Progress in nuclear magnetic resonance spectroscopy.

Comparative Dynamics of Methionine Side-Chain in FMOC-Methionine and in Amyloid Fibrils.

D. Ostrovsky, L. Vugmeyster, 2017, Chemical physics letters.

Beat Vögeli, D. Ostrovsky, C. McKnight, 2018, Journal of Biomolecular NMR.

Optimized purification of a fusion protein by reversed-phase high performance liquid chromatography informed by the linear solvent strength model.

C. Mant, R. Hodges, C. McKnight, 2017, Journal of chromatography. A.

Slow methyl axes motions in perdeuterated villin headpiece subdomain probed by cross-correlated NMR relaxation measurements.

Beat Vögeli, D. Ostrovsky, C. McKnight, 2023, Magnetochemistry.

Deuteron rotating frame relaxation for the detection of slow motions in rotating solids.

D. Ostrovsky, R. Fu, L. Vugmeyster, 2022, Journal of magnetic resonance.

Deuteration of nonexchangeable protons on proteins affects their thermal stability, side‐chain dynamics, and hydrophobicity

C. Mant, R. Hodges, Beat Vögeli, 2020, Protein science : a publication of the Protein Society.

Distance-independent Cross-correlated Relaxation and Isotropic Chemical Shift Modulation in Protein Dynamics Studies.

Beat Vögeli, L. Vugmeyster, 2018, Chemphyschem : a European journal of chemical physics and physical chemistry.

Restricted diffusion of methyl groups in proteins revealed by deuteron NMR: manifestation of intra-well dynamics.

D. Ostrovsky, L. Vugmeyster, 2014, The Journal of chemical physics.

Temperature dependence of fast carbonyl backbone dynamics in chicken villin headpiece subdomain

D. Ostrovsky, L. Vugmeyster, 2011, Journal of biomolecular NMR.

Comparison of fast backbone dynamics at amide nitrogen and carbonyl sites in dematin headpiece C-terminal domain and its S74E mutant

D. Ostrovsky, Y. Li, L. Vugmeyster, 2010, Journal of biomolecular NMR.

Slow motions in chicken villin headpiece subdomain probed by cross-correlated NMR relaxation of amide NH bonds in successive residues.

C. McKnight, L. Vugmeyster, 2008, Biophysical journal.

Temperature-dependent dynamics of the villin headpiece helical subdomain, an unusually small thermostable protein.

D. Raleigh, A. Palmer, C. McKnight, 2002, Journal of molecular biology.

The N-terminal modified Aβ variants enable modulations to the structures and cytotoxicity levels of wild-type Aβ fibrils through cross-seeding.

W. Qiang, Zhi‐Wen Hu, L. Vugmeyster, 2020, ACS chemical neuroscience.

Dynamics of Serine-8 Side-Chain in Amyloid-β Fibrils and Fluorenylmethyloxycarbonyl Serine Amino Acid, Investigated by Solid-State Deuteron NMR.

S. Reed, D. Ostrovsky, L. Vugmeyster, 2020, The journal of physical chemistry. B.

Dynamics of Hydrophobic Core Phenylalanine Residues Probed by Solid-State Deuteron NMR.

W. Xu, A. Lipton, D. Ostrovsky, 2015, The journal of physical chemistry. B.

Beyond the decoupling approximation in the model free approach for the interpretation of NMR relaxation of macromolecules in solution.

D. Raleigh, A. Palmer, L. Vugmeyster, 2003, Journal of the American Chemical Society.

Deuteron Quadrupolar Chemical Exchange Saturation Transfer (Q-CEST) Solid-State NMR for Static Powder Samples: Approach and Applications to Amyloid-β Fibrils.

D. Ostrovsky, R. Fu, L. Vugmeyster, 2019, Chemphyschem : a European journal of chemical physics and physical chemistry.

Effect of Post-Translational Modifications and Mutations on Amyloid-β Fibrils Dynamics at N-Terminus.

D. Ostrovsky, R. Fu, W. Qiang, 2019, Biophysical journal.

Origin of abrupt rise in deuteron NMR longitudinal relaxation times of protein methyl groups below 90 K.

A. Lipton, D. Ostrovsky, L. Vugmeyster, 2013, The journal of physical chemistry. B.

Glassy dynamics of protein methyl groups revealed by deuteron NMR.

D. Ostrovsky, G. Hoatson, R. Vold, 2013, The journal of physical chemistry. B.

Probing the dynamics of a protein hydrophobic core by deuteron solid-state nuclear magnetic resonance spectroscopy.

J. Ford, A. Lipton, D. Ostrovsky, 2009, Journal of the American Chemical Society.

Slow backbone dynamics of chicken villin headpiece subdomain probed by NMR C′N cross‐correlated relaxation

L. Vugmeyster, 2009, Magnetic resonance in chemistry : MRC.

Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale.

Yuefeng Tang, C James McKnight, D. Raleigh, 2003, Journal of the American Chemical Society.

15N R(1ρ) measurements allow the determination of ultrafast protein folding rates [1]

D. Raleigh, C. Kroenke, A. Palmer, 2000 .

(15)N CSA tensors and (15)N-(1)H dipolar couplings of protein hydrophobic core residues investigated by static solid-state NMR.

D. Ostrovsky, R. Fu, L. Vugmeyster, 2015, Journal of magnetic resonance.

N CSA tensors and 15 N – 1 H dipolar couplings of protein hydrophobic core residues investigated by static solid-state NMR

D. Ostrovsky, R. Fu, L. Vugmeyster, 2015 .

Beat Vögeli, D. Ostrovsky, C. McKnight, 2018, Journal of Biomolecular NMR.

Deuteron Solid-State NMR Relaxation Measurements Reveal Two Distinct Conformational Exchange Processes in the Disordered N-Terminal Domain of Amyloid-β Fibrils.

D. Ostrovsky, R. Fu, L. Vugmeyster, 2019, Chemphyschem : a European journal of chemical physics and physical chemistry.

Solvent-Driven Dynamical Crossover in the Phenylalanine Side-Chain from the Hydrophobic Core of Amyloid Fibrils Detected by 2H NMR Relaxation.

D. Ostrovsky, G. Hoatson, W. Qiang, 2017, The journal of physical chemistry. B.

Fast Motions of Key Methyl Groups in Amyloid-β Fibrils.

D. Ostrovsky, G. Hoatson, M. Clark, 2016, Biophysical journal.

Fast Motions of Key Methyl Groups in Amyloid-beta Fibrils

D. Ostrovsky, G. Hoatson, M. Clark, 2018 .

Recent developments in deuterium solid-state NMR for the detection of slow motions in proteins.

L. Vugmeyster, 2021, Solid state nuclear magnetic resonance.

Modulation of aggregation and structural polymorphisms of β-amyloid fibrils in cellular environments by pyroglutamate-3 variant cross-seeding

D. Ostrovsky, Lan Yao, Yan Sun, 2023, The Journal of biological chemistry.

Effect of Cross-Seeding of Wild-Type Amyloid-β1-40 Peptides with Post-translationally Modified Fibrils on Internal Dynamics of the Fibrils Using Deuterium Solid-State NMR.

D. Ostrovsky, L. Vugmeyster, Aryana Rodgers, 2023, The journal of physical chemistry. B.

Deuterium Solid-State NMR Quadrupolar Order Rotating Frame Relaxation with Applications to Amyloid-β Fibrils.

D. Ostrovsky, L. Vugmeyster, 2020, Magnetic resonance in chemistry : MRC.

Comparative dynamics of leucine methyl groups in FMOC-leucine and in a protein hydrophobic core probed by solid-state deuteron nuclear magnetic resonance over 7-324 K temperature range.

J. Ford, A. Lipton, D. Ostrovsky, 2010, The journal of physical chemistry. B.

Basic experiments in 2H static NMR for the characterization of protein side-chain dynamics.

D. Ostrovsky, L. Vugmeyster, 2018, Methods.

Restricted diffusion of methyl groups in proteins revealed by deuteron NMR: manifestation of intra-well dynamics.

D. Ostrovsky, L. Vugmeyster, 2014, The Journal of chemical physics.

Effect of subdomain interactions on methyl group dynamics in the hydrophobic core of villin headpiece protein

D. Ostrovsky, L. Vugmeyster, Tien Do, 2014, Protein science : a publication of the Protein Society.

Freezing of dynamics of a methyl group in a protein hydrophobic core at cryogenic temperatures by deuteron NMR spectroscopy.

J. Ford, A. Lipton, D. Ostrovsky, 2010, Journal of the American Chemical Society.

Deuteron off-resonance rotating frame relaxation for the characterization of slow motions in rotating and static solid-state proteins.

D. Ostrovsky, R. Fu, L. Vugmeyster, 2023, Journal of magnetic resonance.

Deuteron Chemical Exchange Saturation Transfer for the Detection of Slow Motions in Rotating Solids

D. Ostrovsky, R. Fu, L. Vugmeyster, 2021, Frontiers in Molecular Biosciences.