Nuclear-Polarized Hydrogen/Deuterium Molecular Source

2019 ◽  
Vol 50 (5) ◽  
pp. 513-519
Author(s):  
Yu. V. Shestakov ◽  
D. M. Nikolenko ◽  
I. A. Rachek ◽  
D. K. Toporkov ◽  
A. V. Yurchenko
Keyword(s):  
Hydrogen Deuterium ◽  
Molecular Source

Liquid-Phase Peak Force Infrared Microscopy

2020 ◽  
Author(s):  
Haomin Wang ◽  
Joseph M. González-Fialkowski ◽  
Wenqian Li ◽  
Yan Yu ◽  
Xiaoji Xu
Keyword(s):  
Liquid Phase ◽  
Spatial Resolution ◽  
Shear Force ◽  
Polymer Surface ◽  
Surface Damage ◽  
Peak Force ◽  
Infrared Microscopy ◽  
Contact Mode ◽  
Force Microscopy ◽  
Hydrogen Deuterium

Atomic force microscopy-infrared microscopy (AFM-IR) provides a route to bypass Abbe’s diffraction limit through photothermal detections of infrared absorption. With the combination of total internal reflection, AFM-IR can operate in the aqueous phase. However, AFM-IR in contact mode suffers from surface damage from the lateral shear force between the tip and sample, and can only achieve 20~25-nm spatial resolution. Here, we develop the liquid-phase peak force infrared (LiPFIR) microscopy that avoids the detrimental shear force and delivers an 8-nm spatial resolution. The non-destructiveness of the LiPFIR microscopy enables <i>in situ</i> chemical measurement of heterogeneous materials and investigations on a range of chemical and physical transformations, including polymer surface reorganization, hydrogen-deuterium isotope exchange, and ethanol-induced denaturation of proteins. We also perform LiPFIR imaging of the budding site of yeast cell wall in the fluid as a demonstration of biological applications. LiPFIR unleashes the potential of in liquid AFM-IR for chemical nanoscopy.

scholarly journals Serine protease dynamics revealed by NMR analysis of the thrombin-thrombomodulin complex

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Riley B. Peacock ◽  
Taylor McGrann ◽  
Marco Tonelli ◽  
Elizabeth A. Komives
Keyword(s):  
Active Site ◽  
Serine Proteases ◽  
Protein C ◽  
Catalytic Mechanism ◽  
Bond Cleavage ◽  
Peptide Bond ◽  
Peptide Bond Cleavage ◽  
Exchange Mass Spectrometry ◽  
Catalytically Active ◽  
Hydrogen Deuterium

AbstractSerine proteases catalyze a multi-step covalent catalytic mechanism of peptide bond cleavage. It has long been assumed that serine proteases including thrombin carry-out catalysis without significant conformational rearrangement of their stable two-β-barrel structure. We present nuclear magnetic resonance (NMR) and hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments on the thrombin-thrombomodulin (TM) complex. Thrombin promotes procoagulative fibrinogen cleavage when fibrinogen engages both the anion binding exosite 1 (ABE1) and the active site. It is thought that TM promotes cleavage of protein C by engaging ABE1 in a similar manner as fibrinogen. Thus, the thrombin-TM complex may represent the catalytically active, ABE1-engaged thrombin. Compared to apo- and active site inhibited-thrombin, we show that thrombin-TM has reduced μs-ms dynamics in the substrate binding (S1) pocket consistent with its known acceleration of protein C binding. Thrombin-TM has increased μs-ms dynamics in a β-strand connecting the TM binding site to the catalytic aspartate. Finally, thrombin-TM had doublet peaks indicative of dynamics that are slow on the NMR timescale in residues along the interface between the two β-barrels. Such dynamics may be responsible for facilitating the N-terminal product release and water molecule entry that are required for hydrolysis of the acyl-enzyme intermediate.

scholarly journals Unraveling cardiolipin-induced conformational change of cytochrome c through H/D exchange mass spectrometry and quartz crystal microbalance

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Sin-Cih Sun ◽  
Hung-Wei Huang ◽  
Yi-Ting Lo ◽  
Min-Chieh Chuang ◽  
Yuan-Hao Howard Hsu
Keyword(s):  
Mass Spectrometry ◽  
Quartz Crystal Microbalance ◽  
Quartz Crystal ◽  
Interaction Model ◽  
Moderate Increase ◽  
Exchange Mass Spectrometry ◽  
Mitochondrial Regulation ◽  
Crucial Component ◽  
Drastic Increase ◽  
Hydrogen Deuterium

AbstractCardiolipin (CL), a crucial component in inner mitochondrial membranes, interacts with cytochrome c (cyt c) to form a peroxidase complex for the catalysis of CL oxidation. Such interaction is pivotal to the mitochondrial regulation of apoptosis and is affected by the redox state of cyt c. In the present study, the redox-dependent interaction of cyt c with CL was investigated through amide hydrogen/deuterium exchange coupled with mass spectrometry (HDXMS) and quartz crystal microbalance with dissipation monitoring (QCM-D). Ferrous cyt c exhibited a more compact conformation compared with its ferric form, which was supported by the lower number of deuterons accumulated and the greater amplitude reduction on dissipation. Upon association with CL, ferrous cyt c resulted in a moderate increase in deuteration, whereas the ferric form caused a drastic increase of deuteration, which indicated that CL-bound ferric cyt c formed an extended conformation. These results were consistent with those of the frequency (f) − dissipation (D) experiments, which revealed that ferric cyt c yielded greater values of |ΔD/Δf| within the first minute. Further fragmentation analysis based on HDXMS indicated that the effect of CL binding was considerably different on ferric and ferrous cyt c in the C-helix and the Loop 9–24. In ferric cyt c, CL binding affected Met80 and destabilized His18 interaction with heme, which was not observed with ferrous cyt c. An interaction model was proposed to explain the aforementioned results.

scholarly journals Study of Anharmonicity in Zirconium Hydrides Using Inelastic Neutron Scattering and Ab-Initio Computer Modeling

Inorganics ◽  
2021 ◽  
Vol 9 (5) ◽  
pp. 29
Author(s):  
Jiayong Zhang ◽  
Yongqiang Cheng ◽  
Alexander I. Kolesnikov ◽  
Jerry Bernholc ◽  
Wenchang Lu ◽  
...  
Keyword(s):  
Neutron Scattering ◽  
Excited States ◽  
Lattice Dynamics ◽  
Density Functional ◽  
Inelastic Neutron Scattering ◽  
Inelastic Neutron ◽  
Vibrational States ◽  
Functional Theory ◽  
Hydrogen Deuterium ◽  
Zirconium Hydrides

The anharmonic phonon behavior in zirconium hydrides and deuterides, including ϵ-ZrH2, γ-ZrH, and γ-ZrD, has been investigated from aspects of inelastic neutron scattering (INS) and lattice dynamics calculations within the framework of density functional theory (DFT). The harmonic model failed to reproduce the spectral features observed in the experimental data, indicating the existence of anharmonicity in those materials and the necessity of further explanations. Here, we present a detailed study on the anharmonicity in zirconium hydrides/deuterides by exploring the 2D potential energy surface of hydrogen/deuterium atoms and solving the corresponding 2D single-particle Schrödinger equation to obtain the eigenfrequencies, which are then convoluted with the instrument resolution. The convoluted INS spectra qualitatively describe the anharmonic peaks in the experimental INS spectra and demonstrate that the anharmonicity originates from the deviations of hydrogen potentials from quadratic behavior in certain directions; the effects are apparent for the higher-order excited vibrational states, but small for the ground and first excited states.

Hydrogen/Deuterium and 16O/18O-Exchange Mass Spectrometry Boosting the Reliability of Compound Identification

2020 ◽  
Vol 92 (10) ◽  
pp. 6877-6885 ◽  
Author(s):  
Yury Kostyukevich ◽  
Alexander Zherebker ◽  
Alexey Orlov ◽  
Oxana Kovaleva ◽  
Tatyana Burykina ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Compound Identification ◽  
Exchange Mass Spectrometry ◽  
Hydrogen Deuterium
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