22/04/2014 3:22:09 AM GMT
NMR structure of the insulin hexamer More...
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Insulin boost: Definitive speculation
Insulin boost: Definitive speculation
http://www.spectroscopynow.com/common/images/thumbnails/13c29eaa1ae.jpgAfter decades of speculation about exactly how insulin interacts with cells, an international group of scientists (led by NMR pioneer Michael Weiss) has at last demonstrated a mode of action that shows how insulin binds to the cell to allow the cell to transform sugar into energy - and how the insulin molecule then changes shape as a result of this connection.
Source: Spectroscopynow.com
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Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 phosphotyrosine binding domain upon binding to an interleukin 4 receptor phosphopeptide.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 phosphotyrosine binding domain upon binding to an interleukin 4 receptor phosphopeptide.
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[NMR paper] Structure and dynamics of a protein assembly. 1H-NMR studies of the 36 kDa R6 insulin
Structure and dynamics of a protein assembly. 1H-NMR studies of the 36 kDa R6 insulin hexamer.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structure and dynamics of a protein assembly. 1H-NMR studies of the 36 kDa R6 insulin hexamer.
J Mol Biol. 1996 Apr 26;258(1):136-57
Authors: Jacoby E, Hua QX, Stern AS, Frank BH, Weiss MA
The structure and dynamics of the R6 human insulin hexamer are investigated by two- and three-dimensional homonuclear 1H-NMR spectroscopy....
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The solution structure of the isolated B-chain of...
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Authors: Sato A, Nishimura S, Ohkubo T, Kyogoku Y, Koyama S, Kobayashi M, Yasuda T, Kobayashi Y
Human insulin-like growth factor-I (IGF-I) was studied by two-dimensional 1H-NMR spectroscopy. Resonance assignments were obtained for all the backbone protons and almost all of the sidechain protons...
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Solvent conditions where human insulin could be studied by high-resolution NMR were determined. Both low pH and addition of acetonitrile were required to overcome the protein's self-association and to obtain useful spectra. Two hundred eighty-six 1H resonances were located and assigned to specific sites on the protein by using...
NMR structure of the insulin hexamer
Linear Mode
