Related Articles1H- 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 undecapeptide CTTTNSRGTTT in DMSO solution. Nuclear Overhauser enhancement spectroscopy experiments indicated the presence of secondary structures, mainly turn-like structures, which only represent a family, albeit a dominant one, of an ensemble of conformations available to the peptide. Since reverse turns may play an important role as intermediates in protein folding, the experimental observations described here may link the immunological and theoretical approaches to protein folding.
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...
[NMR paper] Extensive 1H NMR resonance assignment of proteins using natural abundance gradient-en
Extensive 1H NMR resonance assignment of proteins using natural abundance gradient-enhanced 13C-1H correlation spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Extensive 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...
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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
...
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[NMR paper] Binding, X-ray and NMR studies of the three A-ring isomers of natural estradiol.
Binding, X-ray and NMR studies of the three A-ring isomers of natural estradiol.
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J Steroid Biochem. 1990 Feb;35(2):219-29
Authors: Palomino E, Heeg MJ, Horwitz JP, Brooks SC
The effect of the position of the phenolic hydroxyl on the conformations of the three A-ring isomers of estradiol, namely, estra-1,3,5(10)-trien-1,17 beta-diol (10), estra-1,3,5(10)-trien-2,17 beta-diol (3), and estra-1,3,5(10)-trien-4,17 beta-diol (6), has been analyzed by...