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01-03-2012 01:42 PM
The relative and regional stabilities of the hamster, mouse, rabbit and bovine prion proteins towards urea unfolding assessed by NMR and CD spectroscopies.
The relative and regional stabilities of the hamster, mouse, rabbit and bovine prion proteins towards urea unfolding assessed by NMR and CD spectroscopies.
The relative and regional stabilities of the hamster, mouse, rabbit and bovine prion proteins towards urea unfolding assessed by NMR and CD spectroscopies.
Biochemistry. 2011 Jul 29;
Authors: Julien O, Chatterjee S, Bjorndahl TC, Sweeting B, Acharya S, Semenchenko V, Chakrabartty A, Pai EF, Wishart DS, Sykes BD, Cashman NR
The residue specific urea-induced unfolding patterns of recombinant...
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08-02-2011 11:40 AM
[NMR paper] Relative stability of protein structures determined by X-ray crystallography or NMR s
Relative stability of protein structures determined by X-ray crystallography or NMR spectroscopy: a molecular dynamics simulation study.
Related Articles Relative stability of protein structures determined by X-ray crystallography or NMR spectroscopy: a molecular dynamics simulation study.
Proteins. 2003 Oct 1;53(1):111-20
Authors: Fan H, Mark AE
The relative stability of protein structures determined by either X-ray crystallography or nuclear magnetic resonance (NMR) spectroscopy has been investigated by using molecular dynamics simulation...
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11-24-2010 09:16 PM
Determination of relative tensor orientations by ?-encoded chemical shift anisotropy/
Determination of relative tensor orientations by ?-encoded chemical shift anisotropy/heteronuclear dipolar coupling 3D NMR spectroscopy in biological solids.
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Phys Chem Chem Phys. 2010 Oct 8;
Authors: Hou G, Paramasivam S, Byeon IJ, Gronenborn AM, Polenova T
In this paper, we present 3D chemical shift anisotropy (CSA)/dipolar coupling correlation experiments, based on ?-encoded...
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10-12-2010 02:52 PM
[NMR paper] The relative orientation of Gla and EGF domains in coagulation factor X is altered by
The relative orientation of Gla and EGF domains in coagulation factor X is altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle X-ray scattering study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles The relative orientation of Gla and EGF domains in coagulation factor X is altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle X-ray scattering study.
Biochemistry. 1996 Sep 10;35(36):11547-59
Authors: Sunnerhagen M, Olah GA, Stenflo J, Forsén S,...
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[U. of Ottawa NMR Facility Blog] E.COSY and the Relative Signs of Coupling Constants
E.COSY and the Relative Signs of Coupling Constants
Spin-spin coupling constants can have values greater than or less than zero. The absolute sign of the coupling constants cannot be discerned from the simple examination of a 1H NMR spectrum. The E.COSY1 (Exclusive COrrelation SpectroscopY) technique is one method which can be used to determine the relative signs of coupling constants. E.COSY is a phase sensitive COSY variant which produces off-diagonal signals showing only the active coupling (i.e. the coupling directly responsible for the cross-peak) as 2x2 antiphase square tetrads...