Overlapping signals in the proton NMR spectra of complex liquids, like foodstuffs and soft drinks, can be processed using a chemometric method, independent component analysis, to extract the spectra of pure components and determine their concentrations.
Unravelling the Conformational Plasticity of the Extracellular Domain of a Prokaryotic nAChR Homologue in Solution by NMR
Unravelling the Conformational Plasticity of the Extracellular Domain of a Prokaryotic nAChR Homologue in Solution by NMR
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi201223u/aop/images/medium/bi-2011-01223u_0002.gif
Biochemistry
DOI: 10.1021/bi201223u
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[NMR paper] Conformational analysis by NMR and distance geometry techniques of a peptide mimetic
Conformational analysis by NMR and distance geometry techniques of a peptide mimetic of the third helix of the Antennapedia homeodomain.
Related Articles Conformational analysis by NMR and distance geometry techniques of a peptide mimetic of the third helix of the Antennapedia homeodomain.
J Pept Res. 2005 Feb;65(2):200-8
Authors: Saviano M, Isernia C, Bassarello C, Di Lello P, Galdiero S, Mierke DF, Benedetti E, Pedone C
The Antennapedia homeodomain structure consists of four helices. The helices II and III are connected by a tripeptide that...
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11-24-2010 11:14 PM
[NMR paper] Detailed NMR analysis of the heme-protein interactions in component IV Glycera dibran
Detailed NMR analysis of the heme-protein interactions in component IV Glycera dibranchiata monomeric hemoglobin-CO.
Related Articles Detailed NMR analysis of the heme-protein interactions in component IV Glycera dibranchiata monomeric hemoglobin-CO.
J Biomol NMR. 1998 Feb;11(2):119-33
Authors: Alam SL, Volkman BF, Markley JL, Satterlee JD
Complete 13C, 15N, and 1H resonance assignments have been obtained for the recombinant, ferrous CO-ligated from of component IV monomeric hemoglobin from Glycera dibranchiata. This 15642 Da myoglobin-like...
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Structure-Independent Analysis of the Breadth of the Positional Distribution of Disor
Structure-Independent Analysis of the Breadth of the Positional Distribution of Disordered Groups in Macromolecules from Order Parameters for Long, Variable-Length Vectors Using NMR Paramagnetic Relaxation Enhancement
Junji Iwahara et al
http://pubs.acs.org//appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1048187/aop/images/medium/ja-2010-048187_0001.gifJournal of the American Chemical Society, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable).
Source: Journal of the American Chemical Society
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[NMR paper] NMR restraint analysis of transforming growth factor alpha: a key component for NMR s
NMR restraint analysis of transforming growth factor alpha: a key component for NMR structure refinement.
Related Articles NMR restraint analysis of transforming growth factor alpha: a key component for NMR structure refinement.
Proteins. 1992 Aug;13(4):306-26
Authors: Brown FK, Hempel JC, Jeffs PW
Structures of the protein, transforming growth factor alpha (TGF-alpha), have been derived from NMR data using distance geometry and subsequent energy refinement. Analysis of the sequential NOE distance bounds using a template algorithm provides a...
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[NMR paper] The mobile loop region of the NAD(H) binding component (dI) of proton-translocating n
The mobile loop region of the NAD(H) binding component (dI) of proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum: complete NMR assignment and effects of bound nucleotides.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The mobile loop region of the NAD(H) binding component (dI) of proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum: complete NMR assignment and effects of bound nucleotides.
Biochim Biophys Acta. 1999...
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[NMR paper] Structural changes in the recombinant, NADP(H)-binding component of proton translocat
Structural changes in the recombinant, NADP(H)-binding component of proton translocating transhydrogenase revealed by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structural changes in the recombinant, NADP(H)-binding component of proton translocating transhydrogenase revealed by NMR spectroscopy.
FEBS Lett. 1999 Mar 5;446(1):127-32
Authors: Quirk PG, Jeeves M, Cotton NP, Smith JK, Jackson BJ
We have analysed 1H, 15N-HSQC spectra of the...
Unravelling proton NMR spectra of foodstuffs with independent component analysis techniques
Overlapping signals in the proton NMR spectra of complex liquids, like foodstuffs and soft drinks, can be processed using a chemometric method, independent component analysis, to extract the spectra of pure components and determine their concentrations.
Linear Mode
