Related ArticlesProbing 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 exchange between all possible environments. The results suggest that nonspecific interactions exist between xenon and the protein exteriors and the data are analyzed in term of parameters which characterize the protein surfaces. The experimental data for horse metmyoglobin are interpreted using a model in which xenon forms a 1:1 complex with the protein and the chemical shift of the complexed xenon is reported (Locci et al., Keystone Symposia "Frontiers of NMR in Molecular Biology VI", Jan. 9--15, 1999, Breckenridge, CO, Abstract E216, p. 53; Locci et al., XeMAT 2000 "Optical Polarization and Xenon NMR of Materials", June 28--30, 2000, Sestri Levante, Italy, p. 46).
Probing the Interaction of Cisplatin with the Human Copper Chaperone Atox1 by Solution and In-Cell NMR Spectroscopy
Probing the Interaction of Cisplatin with the Human Copper Chaperone Atox1 by Solution and In-Cell NMR Spectroscopy
Fabio Arnesano, Lucia Banci, Ivano Bertini, Isabella C. Felli, Maurizio Losacco and Giovanni Natile
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja207346p/aop/images/medium/ja-2011-07346p_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja207346p
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/9nWkAzWuq20
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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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Post-doctoral Associate, Solution NMR Spectroscopy of Proteins at Sanford-burnham Med
Post-doctoral Associate, Solution NMR Spectroscopy of Proteins at Sanford-burnham Medical Research Institute (Orlando, FL)
high resolution NMR data on an 800 MHz Bruker spectrometer. NMR-based strategies will be implemented to delineate ... biologically significant proteins, analyzed interactions by NMR at high resolution, and published peer-reviewed...
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Postdoctoral Associate-Solution NMR Spectroscopy of Proteins at Sanford-burnham Medic
Postdoctoral Associate-Solution NMR Spectroscopy of Proteins at Sanford-burnham Medical Research Institute (Orlando, FL)
high resolution NMR data on an 800 MHz Bruker spectrometer. NMR-based strategies will be implemented to delineate ... biologically significant proteins, analyzed interactions by NMR at high resolution, and published peer-reviewed...
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Postdoctoral Associate-Solution NMR Spectroscopy of Proteins - Sanford-Burnham Medica
Postdoctoral Associate-Solution NMR Spectroscopy of Proteins - Sanford-Burnham Medical Research Institute - Orlando, FL, United States
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Metabolic Signaling and Disease Program at the Sanford-Burnham Medical Research Institute, Orlando, Florida. Sanford-Burnham Medical Research Institute is an independent, not-for-profit biomedical research institution dedicated to advancing the frontiers of scientific knowledge in life sciences and medicine and providing the found...
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[NMR paper] Solution conformations of proline rings in proteins studied by NMR spectroscopy.
Solution conformations of proline rings in proteins studied by NMR spectroscopy.
Related Articles Solution conformations of proline rings in proteins studied by NMR spectroscopy.
J Biomol NMR. 1995 Sep;6(2):123-8
Authors: Cai M, Huang Y, Liu J, Krishnamoorthi R
Three different conformations of proline rings in a protein in solution, Up, Down and Twist, have been distinguished, and stereospecific assignments of the pyrrolidine beta-, gamma- and delta-hydrogens have been made on the basis of 1H-1H vicinal coupling constant patterns and...
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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...