Related ArticlesExtensive 1H NMR resonance assignment of proteins using natural abundance gradient-enhanced 13C-1H correlation spectroscopy.
FEBS Lett. 1993 Nov 1;333(3):251-6
Authors: Medvedeva S, Simorre JP, Brutscher B, Guerlesquin F, Marion D
The reliability and completeness of 1H NMR resonance assignment can be improved by the use of 13C-1H HSQC correlation spectra on unlabelled protein samples using pulsed field gradients. This technique is illustrated on a 5.2 mM sample of the 79 residue Desulfovibrio vulgaris ferrocytochrome c553. Protons attached to the same carbon can be unambiguously paired in a HSQC spectrum. Contrary to 1H, most amino acids exhibit characteristic 13C chemical shift ranges, which can be used for 13C assignment. This technique is especially useful for long side chain residues, such as Gln, Glu, Lys, Arg.
Identifying Guanosine Self Assembly at Natural Isotopic Abundance by High-Resolution 1H and 13C Solid-State NMR Spectroscopy
Identifying Guanosine Self Assembly at Natural Isotopic Abundance by High-Resolution 1H and 13C Solid-State NMR Spectroscopy
Amy L. Webber, Stefano Masiero, Silvia Pieraccini, Jonathan C. Burley, Andrew S. Tatton, Dinu Iuga, Tran N. Pham, Gian Piero Spada and Steven P. Brown
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja206516u/aop/images/medium/ja-2011-06516u_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja206516u
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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Fast NMR Data Acquisition From Bicelles Containing a Membrane-Associated Peptide at Natural-Abundance.
Fast NMR Data Acquisition From Bicelles Containing a Membrane-Associated Peptide at Natural-Abundance.
Fast NMR Data Acquisition From Bicelles Containing a Membrane-Associated Peptide at Natural-Abundance.
J Phys Chem B. 2011 Sep 22;
Authors: Yamamoto K, Vivekanandan S, Ramamoorthy A
Abstract
In spite of recent technological advances in NMR spectroscopy, its low sensitivity continues to be a major limitation particularly for the structural studies of membrane proteins. The need for a large quantity of a membrane protein and acquisition of...
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More AccurateJCHCoupling Measurement in the Presence ofJHHStrong Coupling in Natural Abundance
More AccurateJCHCoupling Measurement in the Presence ofJHHStrong Coupling in Natural Abundance
Publication year: 2011
Source: Journal of Magnetic Resonance, Available online 22 September 2011</br>
Bingwu*Yu, Hugo*van Ingen, Subramanian*Vivekanandan, Christoph*Rademacher, Scott E.*Norris, ...</br>
Jcouplings are essential for measuring RDCs (residual dipolar couplings), now routinely used to deduce molecular structure and dynamics of glycans and proteins. Accurate measurement ofJCHis critical for RDCs to reflect the true structure and dynamics in the molecule of interest. We report...
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A natural and readily available crowding agent: NMR studies of proteins in hen egg white.
A natural and readily available crowding agent: NMR studies of proteins in hen egg white.
A natural and readily available crowding agent: NMR studies of proteins in hen egg white.
Proteins. 2010 Dec 13;
Authors: Martorell G, Adrover M, Kelly G, Temussi PA, Pastore A
In vitro studies of biological macromolecules are usually performed in dilute, buffered solutions containing one or just a few different biological macromolecules. Under these conditions, the interactions among molecules are diffusion limited. On the contrary, in living systems,...
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Configurational assignment of D- and L-isovalines in intact, natural, and synthetic p
Configurational assignment of D- and L-isovalines in intact, natural, and synthetic peptides by 2D-NMR spectroscopy.
Related Articles Configurational assignment of D- and L-isovalines in intact, natural, and synthetic peptides by 2D-NMR spectroscopy.
Chem Biodivers. 2010 Jun;7(6):1612-24
Authors: De Zotti M, Schievano E, Mammi S, Kaptein B, Broxterman QB, Singh SB, Brückner H, Toniolo C
We investigated, by means of 2D-NMR, the naturally occurring and chemically synthesized 16-mer integramides A and B, which belong to a group of bioactive, fungal...
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[NMR paper] 1H- and natural abundance 15N-NMR studies of a derivative of a rabies glycoprotein fr
1H- and natural abundance 15N-NMR studies of a derivative of a rabies glycoprotein fragment.
Related Articles 1H- and natural abundance 15N-NMR studies of a derivative of a rabies glycoprotein fragment.
Biopolymers. 1991 May;31(6):713-23
Authors: Molinari H, Consonni R, Pegna M, Zetta L, Neri P, Niccolai N, Bonci A, Lozzi L, Rustici M, Scarselli M
Using a combination of one- and two-dimensional methods, 1H- and 15N-nmr spectroscopy has been employed to perform the complete assignment and the structural determination of the immunogenic...
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[NMR paper] Assignment of the natural abundance 13C spectrum of proteins using 13C 1H-detected he
Assignment of the natural abundance 13C spectrum of proteins using 13C 1H-detected heteronuclear multiple-bond correlation NMR spectroscopy: structural information and stereospecific assignments from two- and three-bond carbon-hydrogen coupling constants.
Related Articles Assignment of the natural abundance 13C spectrum of proteins using 13C 1H-detected heteronuclear multiple-bond correlation NMR spectroscopy: structural information and stereospecific assignments from two- and three-bond carbon-hydrogen coupling constants.
Biochemistry. 1991 Oct 29;30(43):10457-66
...
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[NMR paper] Assignment of the natural abundance 13C spectrum of proteins using 13C 1H-detected he
Assignment of the natural abundance 13C spectrum of proteins using 13C 1H-detected heteronuclear multiple-bond correlation NMR spectroscopy: structural information and stereospecific assignments from two- and three-bond carbon-hydrogen coupling constants.
Related Articles Assignment of the natural abundance 13C spectrum of proteins using 13C 1H-detected heteronuclear multiple-bond correlation NMR spectroscopy: structural information and stereospecific assignments from two- and three-bond carbon-hydrogen coupling constants.
Biochemistry. 1991 Oct 29;30(43):10457-66
...
Extensive 1H NMR resonance assignment of proteins using natural abundance gradient-en
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