Related ArticlesInteraction between an amantadine analogue and the transmembrane portion of the influenza A M2 protein in liposomes probed by 1H NMR spectroscopy of the ligand.
J Med Chem. 2004 Sep 23;47(20):4975-8
Authors: Kolocouris A, Hansen RK, Broadhurst RW
1H NMR spectroscopy of a fluoroamantadine ligand was used to probe the pH dependence of binding to the transmembrane peptide fragment of the influenza A M2 proton channel (M2TM) incorporated into 1,2-dimyristoyl-sn-glycero-3-phosphocholine liposomes. Above pH 7.5, when M2TM bound the ligand, fluoroamantadine resonances became too broad to be detected. Fluoroamantadine interacted weakly with the liposomes, indicating it may first bind to the bilayer and then block target channels after diffusion across the membrane surface.
13C-Labeled Heparan Sulfate Analogue as a Tool To Study Protein/Heparan Sulfate Interactions by NMR Spectroscopy: Application to the CXCL12? Chemokine
13C-Labeled Heparan Sulfate Analogue as a Tool To Study Protein/Heparan Sulfate Interactions by NMR Spectroscopy: Application to the CXCL12? Chemokine
Ce?dric Laguri, Nicolas Sapay, Jean-Pierre Simorre, Bernhard Brutscher, Anne Imberty, Pierre Gans and Hugues Lortat-Jacob
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja201753e/aop/images/medium/ja-2011-01753e_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja201753e
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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06-09-2011 01:32 AM
13C-labeled heparan sulfate analogue as a tool to study protein/heparan sulfate interaction by NMR spectroscopy. Application to the CXCL12? chemokine.
13C-labeled heparan sulfate analogue as a tool to study protein/heparan sulfate interaction by NMR spectroscopy. Application to the CXCL12? chemokine.
13C-labeled heparan sulfate analogue as a tool to study protein/heparan sulfate interaction by NMR spectroscopy. Application to the CXCL12? chemokine.
J Am Chem Soc. 2011 Jun 2;
Authors: Laguri C, Sapay N, Simorre JP, Brutscher B, Imberty A, Gans P, Lortat-Jacob H
Heparan sulfate, a polysaccharide of the glycosaminoglycan family characterized by a unique level of complexity, has emerged as a key...
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06-04-2011 11:26 AM
[NMR paper] NMR structure determination of a membrane protein with two transmembrane helices in m
NMR structure determination of a membrane protein with two transmembrane helices in micelles: MerF of the bacterial mercury detoxification system.
Related Articles NMR structure determination of a membrane protein with two transmembrane helices in micelles: MerF of the bacterial mercury detoxification system.
Biochemistry. 2005 Apr 5;44(13):5196-206
Authors: Howell SC, Mesleh MF, Opella SJ
The three-dimensional backbone structure of a membrane protein with two transmembrane helices in micelles was determined using solution NMR methods that...
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[NMR paper] Interaction between the type-3 copper protein tyrosinase and the substrate analogue p
Interaction between the type-3 copper protein tyrosinase and the substrate analogue p-nitrophenol studied by NMR.
Related Articles Interaction between the type-3 copper protein tyrosinase and the substrate analogue p-nitrophenol studied by NMR.
J Am Chem Soc. 2005 Jan 19;127(2):567-75
Authors: Tepper AW, Bubacco L, Canters GW
The interaction of the monooxygenating type-3 copper enzyme Tyrosinase (Ty) from Streptomyces antibioticus with its inhibitor p-nitrophenol (pnp) was studied by paramagnetic NMR methods. The pnp binds to oxidized Ty...
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[NMR paper] Investigating the conformational coupling between the transmembrane and cytoplasmic d
Investigating the conformational coupling between the transmembrane and cytoplasmic domains of a single-spanning membrane protein. A 1H-NMR study.
Related Articles Investigating the conformational coupling between the transmembrane and cytoplasmic domains of a single-spanning membrane protein. A 1H-NMR study.
FEBS Lett. 2001 Sep 21;505(3):431-5
Authors: Mousson F, Beswick V, Coïc YM, Huynh-Dinh T, Sanson A, Neumann JM
PMP1 is a 38-residue single-spanning membrane protein whose C-terminal cytoplasmic domain, Y25-F38, is highly positively...
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[NMR paper] Dynamics of the carbohydrate chains attached to the Fc portion of immunoglobulin G as
Dynamics of the carbohydrate chains attached to the Fc portion of immunoglobulin G as studied by NMR spectroscopy assisted by selective 13C labeling of the glycans.
Related Articles Dynamics of the carbohydrate chains attached to the Fc portion of immunoglobulin G as studied by NMR spectroscopy assisted by selective 13C labeling of the glycans.
J Biomol NMR. 1998 Oct;12(3):385-94
Authors: Yamaguchi Y, Kato K, Shindo M, Aoki S, Furusho K, Koga K, Takahashi N, Arata Y, Shimada I
A systematic method for 13C labeling of the glycan of...
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11-17-2010 11:15 PM
[NMR paper] One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11
One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11.7 Tesla.
Related Articles One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11.7 Tesla.
J Protein Chem. 1990 Apr;9(2):129-36
Authors: Dill K, Hu SH, Berman E, Pavia AA, Lacombe JM
One- and two-dimensional nuclear magnetic resonance (NMR) spectroscopy (at 11.7 Tesla) was used to gain some structural and spectral information about glycophorin AM, glycophorin AM tryptic glycopeptide, a related pentapeptide, and two related...