Translational diffusion of macromolecular assemblies measured using transverse relaxation-optimized PFG-NMR.
Translational diffusion of macromolecular assemblies measured using transverse relaxation-optimized PFG-NMR.
Translational diffusion of macromolecular assemblies measured using transverse relaxation-optimized PFG-NMR.
J Am Chem Soc. 2011 Sep 16;
Authors: Horst R, Horwich AL, Wüthrich K
Abstract
ABSTRACT In structural biology, pulsed field gradient (PFG) NMR for characterization of size and hydrodynamic parameters of macromolecular solutes has the advantage over other techniques that the measurements can be recorded with identical solution...
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09-17-2011 08:21 PM
Hydrodynamic dispersion in [Formula: see text] -lactoglobulin gels measured by PGSE NMR.
Hydrodynamic dispersion in -lactoglobulin gels measured by PGSE NMR.
Hydrodynamic dispersion in -lactoglobulin gels measured by PGSE NMR.
Eur Phys J E Soft Matter. 2011 Feb;34(2):1-15
Authors: Fridjonsson EO, Bernin D, Seymour JD, Nydén M, Codd SL
The displacement scale dependent molecular dynamics of solvent water molecules flowing through -lactoglobulin gels are measured by pulse gradient spin echo (PGSE) nuclear magnetic resonance (NMR). Gels formed under different p H conditions generate structures which are characterized by magnetic...
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03-02-2011 11:54 AM
[NMR paper] Water-protein interactions in microcrystalline crh measured by 1H-13C solid-state NMR
Water-protein interactions in microcrystalline crh measured by 1H-13C solid-state NMR spectroscopy.
Related Articles Water-protein interactions in microcrystalline crh measured by 1H-13C solid-state NMR spectroscopy.
J Am Chem Soc. 2003 Nov 5;125(44):13336-7
Authors: Lesage A, Böckmann A
Using solid-state NMR carbon-proton dipolar correlation spectroscopy, we observed hydrogen exchange on the millisecond time scale between water molecules and protein protons in a solid sample. These interactions are shown to be related to important structural...
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11-24-2010 09:16 PM
[NMR paper] Val(659)-->Glu mutation within the transmembrane domain of ErbB-2: effects measured b
Val(659)-->Glu mutation within the transmembrane domain of ErbB-2: effects measured by (2)H NMR in fluid phospholipid bilayers.
Related Articles Val(659)-->Glu mutation within the transmembrane domain of ErbB-2: effects measured by (2)H NMR in fluid phospholipid bilayers.
Biochemistry. 2000 May 30;39(21):6572-80
Authors: Sharpe S, Barber KR, Grant CW
Certain point mutations within the hydrophobic transmembrane domains of class I receptor tyrosine kinases have been associated with oncogenic transformation in vitro and in vivo . An important...
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11-18-2010 09:15 PM
[NMR paper] Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: d
Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: differences in solution and crystal forms of maltodextrin binding protein loaded with beta-cyclodextrin.
Related Articles Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: differences in solution and crystal forms of maltodextrin binding protein loaded with beta-cyclodextrin.
J Mol Biol. 2000 Feb 4;295(5):1265-73
Authors: Skrynnikov NR, Goto NK, Yang D, Choy WY, Tolman JR, Mueller GA, Kay LE
Protein function is often regulated...
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11-18-2010 09:15 PM
[NMR paper] Motional dynamics of residues in a beta-hairpin peptide measured by 13C-NMR relaxatio
Motional dynamics of residues in a beta-hairpin peptide measured by 13C-NMR relaxation.
Related Articles Motional dynamics of residues in a beta-hairpin peptide measured by 13C-NMR relaxation.
Protein Sci. 1998 Mar;7(3):720-9
Authors: Ramirez-Alvarado M, Daragan VA, Serrano L, Mayo KH
Structurally characterizing partially folded peptides is problematic given the nature of their transient conformational states. 13C-NMR relaxation data can provide information on the geometry of bond rotations, motional restrictions, and correlated bond rotations...
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11-17-2010 11:06 PM
[NMR paper] The location of the polyphosphate-binding sites on cytochrome c measured by NMR param
The location of the polyphosphate-binding sites on cytochrome c measured by NMR paramagnetic difference spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles The location of the polyphosphate-binding sites on cytochrome c measured by NMR paramagnetic difference spectroscopy.
Eur J Biochem. 1991 Aug 1;199(3):569-74
Authors: Concar DW, Whitford D, Williams RJ
Analyses of unimolecular electron self-exchange reactions provide...
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08-21-2010 11:12 PM
[NMR paper] The location of the polyphosphate-binding sites on cytochrome c measured by NMR param
The location of the polyphosphate-binding sites on cytochrome c measured by NMR paramagnetic difference spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles The location of the polyphosphate-binding sites on cytochrome c measured by NMR paramagnetic difference spectroscopy.
Eur J Biochem. 1991 Aug 1;199(3):569-74
Authors: Concar DW, Whitford D, Williams RJ
Analyses of unimolecular electron self-exchange reactions provide...
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