Published annually for over three decades, Bruker Almanac has been a tradition in Bruker's history, providing useful information to many scientists around the world. This almanac is now available as a free application for iPhone/iPod touch/iPad that can be downloaded from the iTunes store (download link). Bruker Almanac App provides several handy tables of useful NMR information.
To download the complete Bruker Almanac 2010 as a PDF file with scientific tables and charts and Bruker product guide visit www.bruker.com/almanac
Another NMR-related i-App is from Tim Burrow (University of Toronto). His recently updated Attenuator utility calculates attenuation values: http://itunes.apple.com/ca/app/attenuator/id367216554
Monday, September 27, 2010
Saturday, September 25, 2010
Review in Progress in Nuclear Magnetic Resonance Spectroscopy
A.J. Simpson, D.J. McNally, M.J. Simpson "NMR Spectroscopy in Environmental Research: From Molecular Interactions to Global Processes," Progress in Nuclear Magnetic Resonance Spectroscopy (2010) in press. (Invited Review) http://dx.doi.org/10.1016/j.pnmrs.2010.09.001
Wednesday, September 22, 2010
Biophysical Society 55th Annual Meeting
The 2011 Annual Meeting will be held in the Baltimore Convention Center, Baltimore, Maryland, March 5-9, 2011.
Sunday, October 3, 2010, is the abstract submission deadline and deadline to apply for travel awards and the SRAA competition.
Abstract Submission
http://www.biophysics.org/2011meeting/tabid/2086/Default.aspx
Student, International, Minority, and CPOW Travel Award Applications http://www.biophysics.org/2011meeting/tabid/2171/Default.aspx
Student Research Achievement Award (SRAA) Application http://www.biophysics.org/2011meeting/tabid/2099/Default.aspx
Remember, you MUST be a 2011 Member to submit or sponsor an abstract and to apply for travel awards and the SRAA competition. Members also enjoy reduced registration rates. To join the Society, visit:
http://www.biophysics.org/Membership/JoinNow/tabid/64/Default.aspx
For continually updated Annual Meeting information, visit http://www.biophysics.org/2011meeting
Biophysical Society
9650 Rockville Pike
Bethesda, MD 20814
(301) 634-7114 Phone
(301) 634-7133 Fax
society "at" biophysics.org
Sunday, October 3, 2010, is the abstract submission deadline and deadline to apply for travel awards and the SRAA competition.
Abstract Submission
http://www.biophysics.org/2011meeting/tabid/2086/Default.aspx
Student, International, Minority, and CPOW Travel Award Applications http://www.biophysics.org/2011meeting/tabid/2171/Default.aspx
Student Research Achievement Award (SRAA) Application http://www.biophysics.org/2011meeting/tabid/2099/Default.aspx
Remember, you MUST be a 2011 Member to submit or sponsor an abstract and to apply for travel awards and the SRAA competition. Members also enjoy reduced registration rates. To join the Society, visit:
http://www.biophysics.org/Membership/JoinNow/tabid/64/Default.aspx
For continually updated Annual Meeting information, visit http://www.biophysics.org/2011meeting
Biophysical Society
9650 Rockville Pike
Bethesda, MD 20814
(301) 634-7114 Phone
(301) 634-7133 Fax
society "at" biophysics.org
Wednesday, September 15, 2010
Cover article in Dalton Transactions
David Bryce (University of Ottawa) has written a Perspective for Dalton Transactions about recent advancements in 43Ca NMR spectroscopy and its applications in materials science.
David L. Bryce "Calcium Binding Environments Probed by 43Ca NMR Spectroscopy," Dalton Transactions 39 (2010) 8593-8602. (Cover Article). http://dx.doi.org/10.1039/c0dt00416b
This Perspective is featured on the cover of the current Dalton Transaction issue (2010, #37), and was recently highlighted by SpectroscopyNow.
This is an eighth cover article featuring results obtained using resources of the National Ultrahigh-Field NMR Facility for Solids. See our cover gallery and the complete list of research publications enabled by the Facility here (complete list).
David L. Bryce "Calcium Binding Environments Probed by 43Ca NMR Spectroscopy," Dalton Transactions 39 (2010) 8593-8602. (Cover Article). http://dx.doi.org/10.1039/c0dt00416b
This Perspective is featured on the cover of the current Dalton Transaction issue (2010, #37), and was recently highlighted by SpectroscopyNow.
This is an eighth cover article featuring results obtained using resources of the National Ultrahigh-Field NMR Facility for Solids. See our cover gallery and the complete list of research publications enabled by the Facility here (complete list).
Encyclopedia of Magnetic Resonance: new entries
L.E. Kay, "Structure and Dynamics of Proteins – Big and Small", Encyclopedia of Magnetic Resonance (2010). http://dx.doi.org/10.1002/9780470034590.emrhp1027
W.F. Reynolds, "Heteronuclear Multiple Bond Correlation (HMBC) Spectra", Encyclopedia of Magnetic Resonance (2010). http://dx.doi.org/10.1002/9780470034590.emrstm1176
W.F. Reynolds, "Heteronuclear Multiple Bond Correlation (HMBC) Spectra", Encyclopedia of Magnetic Resonance (2010). http://dx.doi.org/10.1002/9780470034590.emrstm1176
Thursday, September 9, 2010
NMR paper in Science
D.M. Korzhnev, T.L. Religa, W.Banachewicz, A.R. Fersht, L.E. Kay, "A Transient and Low-Populated Protein-Folding Intermediate at Atomic Resolution", Science 329 (2010) 1312-1316. http://dx.doi.org/10.1126/science.1191723
Abstract: "Proteins can sample conformational states that are critical for function but are seldom detected directly because of their low occupancies and short lifetimes. In this work, we used chemical shifts and bond-vector orientation constraints obtained from nuclear magnetic resonance relaxation dispersion spectroscopy, in concert with a chemical shift–based method for structure elucidation, to determine an atomic-resolution structure of an "invisible" folding intermediate of a small protein module: the FF domain. The structure reveals non-native elements preventing formation of the native conformation in the carboxyl-terminal part of the protein. This is consistent with the kinetics of folding in which a well-structured intermediate forms rapidly and then rearranges slowly to the native state. The approach introduces a general strategy for structure determination of low-populated and transiently formed protein states."
This research article by Lewis Kay (University of Toronto) and colleagues is also accompanied by the Science Perspective
H.M. Al-Hashimi, "Exciting Structures", Science 329 (2010) 1295-1296. http://dx.doi.org/10.1126/science.1195571
Abstract: "Proteins can sample conformational states that are critical for function but are seldom detected directly because of their low occupancies and short lifetimes. In this work, we used chemical shifts and bond-vector orientation constraints obtained from nuclear magnetic resonance relaxation dispersion spectroscopy, in concert with a chemical shift–based method for structure elucidation, to determine an atomic-resolution structure of an "invisible" folding intermediate of a small protein module: the FF domain. The structure reveals non-native elements preventing formation of the native conformation in the carboxyl-terminal part of the protein. This is consistent with the kinetics of folding in which a well-structured intermediate forms rapidly and then rearranges slowly to the native state. The approach introduces a general strategy for structure determination of low-populated and transiently formed protein states."
This research article by Lewis Kay (University of Toronto) and colleagues is also accompanied by the Science Perspective
H.M. Al-Hashimi, "Exciting Structures", Science 329 (2010) 1295-1296. http://dx.doi.org/10.1126/science.1195571
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