Related ArticlesProton NMR spin grouping and exchange in dentin.
Biophys J. 1991 Mar;59(3):629-39
Authors: Schreiner LJ, Cameron IG, Funduk N, MiljkoviÄ? L, Pintar MM, Kydon DN
The nuclear magnetic resonance spin-grouping technique has been applied to dentin from human donors of different ages. The apparent T2, T1, and T1 rho have been determined for natural dentin, for dentin which has been dried in vacuum, and for dried dentin which has been rehydrated in an atmosphere with 75% relative humidity. All apparent spin relaxation has been analyzed for exchange between the spin groups in which the dentin protons exist; the analyses incorporate the results of selective inversion recovery T1 measurements which better probe the effects of exchange. The exchange analyses of the high fields and rotating frame spin-lattice relaxation have also been correlated to determine uniquely the inherent relaxation parameters of the proton spin groups constituting the dentin magnetization. The natural dentin contains protons on water, protein, and hydroxy apatite; these spins contribute 50%, 45%, and 5% to the total dentin proton magnetization, respectively. The water exists in three distinct environments, the dynamics of each environment has been modeled. In the natural dentin 30% of the water undergoes uni-axial reorientation. 52% of the water has similar relaxation characteristics to bound water hydrating a large molecule, and the majority of the remaining water acts as bulk water undergoing isotropic reorientation. The results are independent of the age of the donor.
NMR Detection of pH-Dependent Histidine–Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel
NMR Detection of pH-Dependent Histidine–Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel
Fanghao Hu, Klaus Schmidt-Rohr and Mei Hong
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2081185/aop/images/medium/ja-2011-081185_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2081185
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/C3pPoB5_PR8
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10-22-2011 10:16 AM
Water proton spin saturation affects measured protein backboneN spin relaxation rates
Water proton spin saturation affects measured protein backboneN spin relaxation rates
Publication year: 2011
Source: Journal of Magnetic Resonance, Available online 1 October 2011</br>
Kang*Chen, Nico*Tjandra</br>
Protein backboneN NMR spin relaxation rates are useful in characterizing the protein dynamics and structures. To observe the protein nuclear-spin resonances a pulse sequence has to include a water suppression scheme. There are two commonly employed methods, saturating or dephasing the water spins with pulse field gradients and keeping them unperturbed with flip-back pulses....
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10-02-2011 08:25 AM
Mathematical treatment of adiabatic fast passage pulses for the computation of nuclear spin relaxation rates in proteins with conformational exchange
Mathematical treatment of adiabatic fast passage pulses for the computation of nuclear spin relaxation rates in proteins with conformational exchange
Abstract Although originally designed for broadband inversion and decoupling in NMR spectroscopy, recent methodological developments have introduced adiabatic fast passage (AFP) pulses into the field of protein dynamics. AFP pulses employ a frequency sweep, and have not only superior inversion properties with respect to offset effects, but they are also easily implemented into a pulse sequence. As magnetization is dragged from the +z to...
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09-30-2011 08:01 PM
Challenges in numerical simulations of solid-state NMR experiments: Spin exchange pulse sequences.
Challenges in numerical simulations of solid-state NMR experiments: Spin exchange pulse sequences.
Challenges in numerical simulations of solid-state NMR experiments: Spin exchange pulse sequences.
Solid State Nucl Magn Reson. 2011 Feb 1;
Authors: Vosegaard T
While simulations are essential for interpretation of solid-state NMR experiments, large spin systems involved in e.g. spin-diffusion experiments and/or dynamic effects like chemical exchange pose great challenges for the numerical simulations, where we typically want to include effects of...
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02-19-2011 06:02 PM
[NMR paper] High-sensitivity observation of dipolar exchange and NOEs between exchangeable proton
High-sensitivity observation of dipolar exchange and NOEs between exchangeable protons in proteins by 3D solid-state NMR spectroscopy.
Related Articles High-sensitivity observation of dipolar exchange and NOEs between exchangeable protons in proteins by 3D solid-state NMR spectroscopy.
J Am Chem Soc. 2003 Nov 26;125(47):14222-3
Authors: Paulson EK, Morcombe CR, Gaponenko V, Dancheck B, Byrd RA, Zilm KW
A highly sensitive new 1H-detected 3D solid-state NMR method is described for characterizing 1H-1H spin exchange in nanocrystalline samples of...
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[NMR paper] Imino proton exchange provides an 1H-NMR footprint of protein-DNA interactions: gener
Imino proton exchange provides an 1H-NMR footprint of protein-DNA interactions: general strategy and application to the SRY HMG box.
Related Articles Imino proton exchange provides an 1H-NMR footprint of protein-DNA interactions: general strategy and application to the SRY HMG box.
J Biomol Struct Dyn. 1995 Oct;13(2):261-8
Authors: Weiss MA, King CY
A novel 1H nuclear magnetic resonance (NMR) strategy for "footprinting" specific protein-DNA target sites is demonstrated. Relative rates of site-specifc imino-proton exchange in the free and bound...
[NMR paper] Comparison of amide proton exchange in reduced and oxidized Rhodobacter capsulatus cy
Comparison of amide proton exchange in reduced and oxidized Rhodobacter capsulatus cytochrome c2: a 1H-15N NMR study.
Related Articles Comparison of amide proton exchange in reduced and oxidized Rhodobacter capsulatus cytochrome c2: a 1H-15N NMR study.
J Biomol NMR. 1991 Jul;1(2):145-54
Authors: Gooley PR, Zhao D, MacKenzie NE
The hydrogen-deuterium exchange rates of the reduced and oxidized forms of Rhodobacter capsulatus cytochrome c2 were studied by 1H-15N homonuclear multiple quantum correlation spectroscopy. Minimal differences were...