[NMR paper] (15)N and (1)H Solid-State NMR Investigation of a Canonical Low-Barrier Hydrogen-Bond Compound: 1,8-bis(dimethylamino) Naphthalene.
(15)N and (1)H Solid-State NMR Investigation of a Canonical Low-Barrier Hydrogen-Bond Compound: 1,8-bis(dimethylamino) Naphthalene.
(15)N and (1)H Solid-State NMR Investigation of a Canonical Low-Barrier Hydrogen-Bond Compound: 1,8-bis(dimethylamino) Naphthalene.
J Phys Chem B. 2015 Aug 5;
Authors: White PB, Hong M
Abstract
Strong or low-barrier hydrogen bonds have been often proposed in proteins to explain enzyme catalysis and proton transfer reactions. So far 1H chemical shifts and scalar couplings have been used as the main...
[NMR paper] Diazole-based powdered cocrystal featuring a helical hydrogen-bonded network: Structure determination from PXRD, solid-state NMR and computer modeling.
Diazole-based powdered cocrystal featuring a helical hydrogen-bonded network: Structure determination from PXRD, solid-state NMR and computer modeling.
Related Articles Diazole-based powdered cocrystal featuring a helical hydrogen-bonded network: Structure determination from PXRD, solid-state NMR and computer modeling.
Solid State Nucl Magn Reson. 2014 Dec 30;
Authors: Sardo M, Santos SM, Babaryk AA, López C, Alkorta I, Elguero J, Claramunt RM, Mafra L
Abstract
We present the structure of a new equimolar 1:1 cocrystal formed by...
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[NMR paper] Determining hydrogen-bond interactions in spider silk with 1H-13C HETCOR fast MAS solid-state NMR and DFT proton chemical shift calculations.
Determining hydrogen-bond interactions in spider silk with 1H-13C HETCOR fast MAS solid-state NMR and DFT proton chemical shift calculations.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Determining hydrogen-bond interactions in spider silk with 1H-13C HETCOR fast MAS solid-state NMR and DFT proton chemical shift calculations.
Chem Commun (Camb). 2013 Jul 28;49(59):6680-2
Authors: Holland GP, Mou Q, Yarger JL
Abstract
Two-dimensional (2D) (1)H-(13)C...
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01-18-2014 11:31 AM
[NMR paper] Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
Related Articles Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
J Biomol NMR. 2005 Jul;32(3):195-207
Authors: Böckmann A, Juy M, Bettler E, Emsley L, Galinier A, Penin F, Lesage A
We report site-resolved observation of hydrogen exchange in the micro-crystalline protein Crh. Our approach is based on the use of proton T2' -selective 1H-13C-13C correlation spectra for...
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12-01-2010 06:56 PM
[NMR paper] Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colic
Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colicin Ia channel-forming domain.
Related Articles Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colicin Ia channel-forming domain.
Biochemistry. 2001 Jun 26;40(25):7662-74
Authors: Huster D, Xiao L, Hong M
Solid-state NMR spectroscopy was employed to study the molecular dynamics of the colicin Ia channel domain in the soluble and membrane-bound states. In the soluble state, the protein executes small-amplitude librations (with...
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11-19-2010 08:32 PM
[NMR paper] 1H NMR investigation of the distal hydrogen bonding network and ligand tilt in the cy
1H NMR investigation of the distal hydrogen bonding network and ligand tilt in the cyanomet complex of oxygen-avid Ascaris suum hemoglobin.
Related Articles 1H NMR investigation of the distal hydrogen bonding network and ligand tilt in the cyanomet complex of oxygen-avid Ascaris suum hemoglobin.
J Biol Chem. 1999 Nov 5;274(45):31819-26
Authors: Xia Z, Zhang W, Nguyen BD, Mar GN, Kloek AP, Goldberg DE
The O(2)-avid hemoglobin from the parasitic nematode Ascaris suum exhibits one of the slowest known O(2) off rates. Solution (1)H NMR has been...
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[NMR paper] Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel
Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers.
Related Articles Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers.
Protein Sci. 1998 Feb;7(2):342-8
Authors: Kim Y, Valentine K, Opella SJ, Schendel SL, Cramer WA
The colicin E1 channel polypeptide was shown to be organized anisotropically in membranes by solid-state NMR analysis of samples of uniformly 15N-labeled protein in oriented planar phospholipid bilayers. The 190...
HighField Solid-State NMR Spectroscopy Investigation of 15N-Labeled Rosette Nanotubes: Hydrogen Bond Network and Channel-Bound Water
Linear Mode
