Related ArticlesProbing a CMP-Kdn synthetase by 1H, 31P, and STD NMR spectroscopy.
Biochem Biophys Res Commun. 2005 Feb 11;327(2):565-70
Authors: Haselhorst T, Münster-Kühnel AK, Stolz A, Oschlies M, Tiralongo J, Kitajima K, Gerardy-Schahn R, von Itzstein M
CMP-Kdn synthetase catalyses the reaction of sialic acids (Sia) and cytidine-5'-triphosphate (CTP) to the corresponding activated sugar nucleotide CMP-Sia and pyrophosphate PP(i). STD NMR experiments of a recombinant nucleotide cytidine-5'-monophosphate-3-deoxy-d-glycero-d-galacto-nonulosonic acid synthetase (CMP-Kdn synthetase) were performed to map the binding epitope of the substrate CTP and the product CMP-Neu5Ac. The STD NMR analysis clearly shows that the anomeric proton of the ribose moiety of both investigated compounds is in close proximity to the protein surface and is likely to play a key role in the binding process. The relative rates of the enzyme reaction, derived from (1)H NMR signal integrals, show that Kdn is activated at a rate 2.5 and 3.1 faster than Neu5Ac and Neu5Gc, respectively. Furthermore, proton-decoupled (31)P NMR spectroscopy was successfully used to follow the enzyme reaction and clearly confirmed the appearance of CMP-Sia and the inorganic pyrophosphate by-product.
[NMR paper] Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
Related Articles Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
J Am Chem Soc. 2005 Sep 28;127(38):13110-1
Authors: Soubias O, Gawrisch K
We studied the interaction of mono- and polyunsaturated phosphatidylcholines with rhodopsin by 1H NMR saturation transfer difference spectroscopy with magic angle spinning (STD-MAS NMR). The results indicate a strong preference for interaction of rhodopsin with the...
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[NMR paper] Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy.
Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy.
Related Articles Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy.
J Biol Chem. 2004 Feb 13;279(7):5699-707
Authors: Olofsson A, Ippel JH, Wijmenga SS, Lundgren E, Ohman A
The human plasma protein transthyretin (TTR) may form fibrillar protein deposits that are associated with both inherited and idiopathic amyloidosis. The present study utilizes solution nuclear magnetic resonance spectroscopy, in combination with...
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[NMR paper] Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy.
Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy.
Related Articles Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy.
Proc Natl Acad Sci U S A. 2002 Jun 25;99(13):8648-53
Authors: Ippel JH, Olofsson A, Schleucher J, Lundgren E, Wijmenga SS
Amyloid is the result of an anomalous protein and peptide aggregation, leading to the formation of insoluble fibril deposits. At present, 18 human diseases have been associated with amyloid deposits-e.g., Alzheimer's disease and Prion-transmissible...
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[NMR paper] Probing proteins in solution by (129)Xe NMR spectroscopy.
Probing proteins in solution by (129)Xe NMR spectroscopy.
Related Articles Probing proteins in solution by (129)Xe NMR spectroscopy.
J Magn Reson. 2001 Jun;150(2):167-74
Authors: Locci E, Dehouck Y, Casu M, Saba G, Lai A, Luhmer M, Reisse J, Bartik K
The interaction of xenon with different proteins in aqueous solution is investigated by (129)Xe NMR spectroscopy. Chemical shifts are measured in horse metmyoglobin, hen egg white lysozyme, and horse cytochrome c solutions as a function of xenon concentration. In these systems, xenon is in fast...
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[NMR paper] Probing carbohydrate-protein interactions by high-resolution NMR spectroscopy.
Probing carbohydrate-protein interactions by high-resolution NMR spectroscopy.
Related Articles Probing carbohydrate-protein interactions by high-resolution NMR spectroscopy.
Adv Exp Med Biol. 1998;435:29-38
Authors: Homans SW, Field RA, Milton MJ, Probert M, Richardson JM
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[NMR paper] Probing the structure and interactions of crystallin proteins by NMR spectroscopy.
Probing the structure and interactions of crystallin proteins by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Probing the structure and interactions of crystallin proteins by NMR spectroscopy.
Prog Retin Eye Res. 1999 Jul;18(4):431-62
Authors: Carver JA
The lens is composed primarily of proteins, the crystallins, at high concentration whose structure and interactions are responsible for lens transparency. As there is no protein turnover in the...