The Human Metabolome Database (HMDB) is a freely available electronic database containing detailed information about small molecule metabolites found in the human body. It is intended to be used for applications in metabolomics, clinical chemistry, biomarker discovery and general education.
HMDB is supported by David Wishart, Departments of Computing Science & Biological Sciences, University of Alberta. HMDB is also supported by the Metabolomics Innovation Centre, a Genome Canada-funded core facility serving the scientific community and industry with world-class expertise and cutting-edge technologies in metabolomics. Funding is provided by Genome Alberta and Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government.
Just announced version 3.0 of the HMDB has been significantly expanded and enhanced over the 2009 release (version 2.0). In particular, the number of annotated metabolite entries has grown from 6500 to more than 37,166. This enormous expansion is a result of the inclusion of both “Confirmed” metabolites (those with measured concentrations or experimental confirmation of their existence) and “Expected” metabolites (those for which biochemical pathways are known or human intake/exposure is frequent but the compound has yet to be detected in the body). The latest release also has greatly increased the number of metabolites with biofluid or tissue concentration data, the number of compounds with reference spectra and the number of data fields per entry. In addition to this expansion in data quantity, new database visualization tools and new data content has been added or enhanced. These include better spectral viewing tools, more powerful chemical substructure searches, an improved chemical taxonomy and better, more interactive pathway maps. Among other database functions, NMR Search allows users to submit peak lists from 1H or 13C NMR spectra (both pure and mixtures) and to have these peak lists compared to the NMR libraries contained in the HMDB. This allows the identification of metabolites from mixtures via NMR spectroscopy.
For more information visit http://www.hmdb.ca/
A. Sutrisno, V.V. Terskikh, Q. Shi, Z. Song, J. Dong, S.Y. Ding, W. Wang, B.R. Provost, T.D. Daff, T.K. Woo, and Y. Huang, "Characterization of Zn-containing MOFs by Solid-state 67Zn NMR and Computational Modeling," Chemistry - A European Journal 18 (2012) 12251–12259. http://dx.doi.org/10.1002/chem.201201563
Solid-state magic-angle spinning 67Zn NMR spectra of Zn-containing metal–organic frameworks were obtained at an ultrahigh magnetic field of 21.1 T. In combination with molecular modeling, 67Zn NMR data can provide information on the dynamics and distribution of guest species.
MOFs: NMR reveals inner secrets, read the highlights of this project on SpectroscopyNow.com written by David Bradley
This cover article features results obtained using the 21.1 T solid-state NMR spectrometer at the National Ultrahigh-Field NMR Facility for Solids (Ottawa, ON). If you are interested in using this spectrometer in your research please contact the Facility manager http://nmr900.ca
January 6-11, 2013, Stowe, Vermont, U.S.
Organizers: Mei Hong (Iowa State), Chad Rienstra (UIUC), and Bob Griffin (MIT)
Dear colleagues, We invite you to encourage your students, postdocs, and associates to attend the 3rd Winter School on Biomolecular Solid-State NMR, to be held on Jan 6-11, 2013, in Stowe, Vermont. Similar to the two previous, very successful, Winter Schools
http://web.mit.edu/fbml/winterschool2008/Winterschool2008.html
This pedagogical meeting, unique in North America, is aimed at students and postdocs in the field of biological solid-state NMR, as well as more senior scientists in related fields who are interested in entering this vibrant field. Our goals are to foster the scientific development of the next generation of North American biological solid-state NMR spectroscopists and to encourage information sharing and collaborations among research groups.
Topics in the 3rd Winter School include:
- Basics of solid-state NMR: orientation dependence, density operators, average Hamiltonian theory, dipolar and CSA recoupling
- Multidimensional correlation techniques: resonance assignment and structure determination
- Theory of polarization transfer and dipolar decoupling
- Pushing the sensitivity envelope: dynamic nuclear polarization
- Solid-state NMR techniques for measuring distances, torsion angles, dynamics and orientations of diamagnetic and paramagnetic systems, for both spin-1/2 and quadrupolar nuclei
- Beating the 800-pound gorilla: NMR of membrane-bound proteins
- Devil in the details: methods for protein expression, isotopic labeling, and preparation of MAS and oriented-membrane samples
- Numerical simulations and structure calculation methods
- NMR probe design
Lectures and problem-solving sessions will be held in the mornings, late afternoons, and evenings, with time for recreation in the early afternoon.
Speakers: The following people have accepted to give lectures
Tim Cross (Florida State)
Matthias Ernst (ETH)
Phil Grandinetti (Ohio State)
Bob Griffin (MIT)
Mei Hong (Iowa State)
Yoshitaka Ishii (U Illinois Chicago)
Chris Jaroniec (Ohio State)
Ann McDermott (Columbia)
Stanley Opella (UCSD)
Chad Rienstra (UIUC)
Klaus Schmidt-Rohr (Iowa State)
Robert Tycko (NIH)
Venue and transportation: The meeting will be held at the Inn at the Mountain in Stowe http://www.stowe.com/plan/groups/stowe-mountain-resort-the-inn-at-the-mountain/
Stowe is easily accessible from airports in Burlington, VT, Manchester, NH, and Boston, MA.
Cost: Room and board will be free for attendees. The registration fee is $325 for academic attendees and $600 for industrial attendees. We anticipate space for about 75-80 people.
Application: Interested students and postdocs should send the following application material as PDF attachments to [mhong "at" iastate.edu]
1. CV and publication list (for the purpose of room assignment, please indicate your gender in the CV)
2. A one-page description of the current research
3. A one-page letter of recommendation from the current research advisor. (In the case of a senior scientist, a brief explanation of your motivations can substitute for a letter of recommendation.)
The deadline for the application is Friday, Oct 26. Given the space limitation and the previous strong interest in this meeting, applications received after the above date may not be accommodated.
Please distribute this announcement to members of your research group as well as to other colleagues who may be interested in attending or sending their group members.
We look forward to welcoming you in Stowe next January,
Mei, Chad, and Bob
------------------------------------------
Mei Hong, Professor of Chemistry
Department of Chemistry, Gilman
1605 Iowa State University
Ames, IA 50011
Tel: 515-294-3521, Fax: 515-294-0105
Web site: http://www.public.iastate.edu/~hongweb/
the 25th MOOT NMR Minisymposium will be held at Université Laval in Quebec City on October 20-21, 2012.
The instructions for abstract submission (oral and poster presentations) are now available on the MOOT web site. Please submit your abstract before October 1st deadline.
http://nmr.ulaval.ca/moot/abstract.html
The talks and poster session will be held in Pavillon Alexandre-Vachon at Université Laval. The banquet will be held at the Morrin Centre in historical old Quebec City. This is the site of the city's first prison, built over 200 years ago, as well as the site of the Morrin College from 1862-1902. http://nmr.ulaval.ca/moot/location.html
If you have comments, inquiries, or would like to be added to the MOOT mailing list, please send a message to [mootnmr "at" gmail.com].
We are looking forward to seeing you in Quebec City in October.
Michèle Auger et Stéphane Gagné
25th MOOT NMR Minisymposium
October 20-21, 2012
Université Laval
Québec City
http://www.mootnmr.org
G. Jansen, P. Määttänen, A.Y. Denisov, L. Scarffe, B. Schade, H. Balghi, K. Dejgaard, L.Y. Chen, W.J. Muller, K. Gehring and D.Y. Thomas, "An interaction map of ER chaperones and foldases," Molecular & Cellular Proteomics 11 (2012) 710-723. (Cover article) http://dx.doi.org/10.1074/mcp.M111.016550