When you catch influenza, the virus hijacks the inner workings of your cells to make copies of itself. The copies accumulate in viral buds that then break free from the host cell to infect another host. Researchers at Massachusetts Institute of Technology have now used solid-state nuclear magnetic resonance (NMR) spectroscopy to obtain a clear picture of how these buds pinch off from the host cell membrane.
[NMR paper] NMR Meets Tau: Insights into Its Function and Pathology.
NMR Meets Tau: Insights into Its Function and Pathology.
NMR Meets Tau: Insights into Its Function and Pathology.
Biomolecules. 2016;6(2)
Authors: Lippens G, Landrieu I, Smet C, Huvent I, Gandhi NS, Gigant B, Despres C, Qi H, Lopez J
Abstract
In this review, we focus on what we have learned from Nuclear Magnetic Resonance (NMR) studies on the neuronal microtubule-associated protein Tau. We consider both the mechanistic details of Tau: the tubulin relationship and its aggregation process. Phosphorylation of Tau is intimately...
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06-25-2016 03:16 PM
Unravelling Helicobacter: Bactofilin insights from NMR
Unravelling Helicobacter: Bactofilin insights from NMR
http://www.spectroscopynow.com/common/images/thumbnails/15186afbbaf.jpgA novel approach to solid-state NMR spectroscopy has allowed researchers to unravel structural details of bactofilin from the ulcer-causing corkscrew bacterium, Helicobacter pylori.
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12-15-2015 07:47 AM
Magnetic insights: Playing the percentages
Magnetic insights: Playing the percentages
http://www.spectroscopynow.com/common/images/thumbnails/13fbe274632.jpgAn international research team has shown that one-dimensional molecular conducting wires can be switched to an insulating state using a weak magnetic field even at room temperature. The finding might offer new insights into the innate navigation systems of migratory birds as well as leading to new technology for magnetic field sensors, inexpensive touch screen displays and high-density magnetic storage for smartphones and other portable devices.
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07-15-2013 07:16 AM
NMR insights into protein allostery
NMR insights into protein allostery
15 March 2012
Publication year: 2012
Source:Archives of Biochemistry and Biophysics, Volume 519, Issue 2</br>
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Allosterism is one of nature’s principal methods for regulating protein function. Allosterism utilizes ligand binding at one site to regulate the function of the protein by modulating the structure and dynamics of a distant binding site. In this review, we first survey solution NMR techniques and how they may be applied to the study of allostery. Subsequently, we describe several examples of application of NMR to protein...
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02-03-2013 10:13 AM
[NMR paper] Insights into the mechanism of heterodimerization from the 1H-NMR solution structure
Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper.
Related Articles Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper.
J Mol Biol. 1998 Aug 7;281(1):165-81
Authors: Lavigne P, Crump MP, Gagné SM, Hodges RS, Kay CM, Sykes BD
The oncoprotein c-Myc (a member of the helix-loop-helix-leucine zipper (b-HLH-LZ) family of transcription factors) must heterodimerize with the b-HLH-LZ Max...
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11-17-2010 11:15 PM
[NMR paper] Insights into protein folding from NMR.
Insights into protein folding from NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--arjournals.annualreviews.org-images-AnnualReviews100x25.gif Related Articles Insights into protein folding from NMR.
Annu Rev Phys Chem. 1996;47:369-95
Authors: Dyson HJ, Wright PE
NMR has emerged as an important tool for studies of protein folding because of the unique structural insights it can provide into many aspects of the folding process. Applications include measurements of kinetic folding events and structural characterization of folding...