Two independent research collaborations have released highly detailed maps of the human proteome in the same publication, identifying a high proportion of the proteins encoded by the human genome.
[NMR paper] Stoichiometric relationship between Na(+) ions transported and glucose consumed in human erythrocytes: Bayesian analysis of (23)Na and (13)C NMR time course data.
Stoichiometric relationship between Na(+) ions transported and glucose consumed in human erythrocytes: Bayesian analysis of (23)Na and (13)C NMR time course data.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Stoichiometric relationship between Na(+) ions transported and glucose consumed in human erythrocytes: Bayesian analysis of (23)Na and (13)C NMR time course data.
Biophys J. 2013 Apr 16;104(8):1676-84
Authors: Puckeridge M, Chapman BE, Conigrave AD, Grieve SM,...
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10-31-2013 02:18 PM
Identifying secondary structures in proteins using NMR chemical shift 3D correlation maps
Identifying secondary structures in proteins using NMR chemical shift 3D correlation maps
Available online 18 March 2013
Publication year: 2013
Source:Journal of Molecular Structure</br>
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NMR chemical shifts are accurate indicators of molecular environment and have been extensively used as aids in protein structure determination. This work focuses on creating empirical 3D correlation maps of backbone chemical shift nuclei for use as identifiers of secondary structure elements in proteins. A correlated database of backbone nuclei chemical shifts was constructed from...
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03-19-2013 12:58 AM
Long-term stability of human proteome
Long-term stability of human proteome
http://www.spectroscopynow.com/common/images/thumbnails/13be29897a7.jpgThe abundances of 31 major proteins in human plasma, measured by selected reaction monitoring mass spectrometry, remained remarkably steady over 4 months, strengthening their case to be used as disease biomarkers.
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02-03-2013 09:08 AM
[NMR900 blog] "Anarchy in the proteome" - interview with Julie Forman-Kay
"Anarchy in the proteome" - interview with Julie Forman-Kay
Julie Forman-Kay (Toronto) speaks about her research in disordered proteins in a podcast interview to the Chemistry World. Available for download at
Chemistry World Podcast, August 2011, "6.05-13.00 Julie Forman-Kay reveals that disordered, unfolded proteins are much more functional and much more common than previously thought"
http://www.rsc.org/chemistryworld/podcast/CWpodcast.asp
Part of this interview is also featured in the printed August 2011 issue of the Chemistry World (subscription required): M. Gross "Anarchy in...
[NMR paper] Dipolar Waves as NMR maps of helices in proteins.
Dipolar Waves as NMR maps of helices in proteins.
Related Articles Dipolar Waves as NMR maps of helices in proteins.
J Magn Reson. 2003 Aug;163(2):288-99
Authors: Mesleh MF, Opella SJ
Dipolar Waves describe the periodic variation in the magnitudes of dipolar couplings in the backbone of a protein as a function of residue number. They provide a direct link between experimental measurements of dipolar couplings in aligned samples and the periodicity inherent in regular secondary structure elements. It is possible to identify the residues in a...
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11-24-2010 09:16 PM
[NMR paper] Dipolar waves as NMR maps of protein structure.
Dipolar waves as NMR maps of protein structure.
Related Articles Dipolar waves as NMR maps of protein structure.
J Am Chem Soc. 2002 Apr 24;124(16):4206-7
Authors: Mesleh MF, Veglia G, DeSilva TM, Marassi FM, Opella SJ
The anisotropy of nuclear spin interactions results in a unique mapping of structure to the resonance frequencies and split tings observed in NMR spectra, however, the determination of molecular structure from experimentally measured spectral parameters is complicated by angular ambiguities resulting from the symmetry properties...
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11-24-2010 08:49 PM
[NMR paper] Internal motion time scales of a small, highly stable and disulfide-rich protein: a 1
Internal motion time scales of a small, highly stable and disulfide-rich protein: a 15N, 13C NMR and molecular dynamics study.
Related Articles Internal motion time scales of a small, highly stable and disulfide-rich protein: a 15N, 13C NMR and molecular dynamics study.
J Biomol NMR. 1999 May;14(1):47-66
Authors: Guenneugues M, Gilquin B, Wolff N, Ménez A, Zinn-Justin S
Motions of the backbone C alpha H alpha and threonine C beta H beta bonds of toxin alpha were investigated using natural abundance 13C NMR and molecular dynamics. Measurement...
Two highly detailed maps of the human proteome released at same time
Two independent research collaborations have released highly detailed maps of the human proteome in the same publication, identifying a high proportion of the proteins encoded by the human genome.
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