Related ArticlesHigh-resolution polypeptide structure in a lamellar phase lipid environment from solid state NMR derived orientational constraints.
Structure. 1997 Dec 15;5(12):1655-69
Authors: Ketchem R, Roux B, Cross T
BACKGROUND: Solid-state nuclear magnetic resonance (NMR) spectroscopy provides novel structural constraints from uniformly aligned samples. These orientational constraints orient specific atomic sites with respect to the magnetic field direction and the unique molecular axis of alignment. Solid-state NMR is uniquely and ideally suited for providing such structural constraints on polypeptides and proteins in a lamellar phase lipid environment. Membrane protein structure represents a great challenge for structural biologists; a new approach for characterizing high resolution three-dimensional structure in such an environment is needed. RESULTS: The optimal use of orientational constraints for defining three-dimensional structures is demonstrated with the elucidation of the gramicidin A channel structure at high resolution. Initial structures are refined against both the experimental constraints and the CHARMM energy using a novel simulated-annealing protocol to define torsion angle solutions with an error bar of approximately +/- 5 degrees. CONCLUSIONS: This analysis results in the determination of a high-resolution, time averaged structure of gramicidin A obtained in a lipid bilayer environment above the gel-to-liquid crystalline phase transition temperature. It is demonstrated that solid-state NMR can be used to establish polypeptide, and potentially protein, structures in such an environment. Furthermore, this high-resolution structure is demonstrated to provide new insights into polypeptide function. For the gramicidin A channel the roles of the indole groups that facilitate ion transport and details of the cation solvation environment provided by the amide oxygens are characterized.
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment
Abstract Overexpression of isotope-labeled multi-spanning eukaryotic membrane proteins for structural NMR studies is often challenging. On the one hand, difficulties with achieving proper folding, membrane insertion, and native-like post-translational modifications frequently disqualify bacterial expression systems. On the other hand, eukaryotic cell cultures can be prohibitively expensive. One of the viable alternatives,...
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Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
J Biomol NMR. 2011 Jan 19;
Authors: Fan Y, Shi L, Ladizhansky V, Brown LS
Overexpression of isotope-labeled multi-spanning eukaryotic membrane proteins for structural NMR studies is often challenging. On the one hand, difficulties...
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01-21-2011 01:22 AM
[NMR paper] Anomalous diffusion in a gel-fluid lipid environment: a combined solid-state NMR and
Anomalous diffusion in a gel-fluid lipid environment: a combined solid-state NMR and obstructed random-walk perspective.
Related Articles Anomalous diffusion in a gel-fluid lipid environment: a combined solid-state NMR and obstructed random-walk perspective.
Biophys J. 2004 Oct;87(4):2456-69
Authors: Arnold A, Paris M, Auger M
Lateral diffusion is an essential process for the functioning of biological membranes. Solid-state nuclear magnetic resonance (NMR) is, a priori, a well-suited technique to study lateral diffusion within a heterogeneous...
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11-24-2010 10:01 PM
[NMR paper] Structure of gramicidin a in a lipid bilayer environment determined using molecular d
Structure of gramicidin a in a lipid bilayer environment determined using molecular dynamics simulations and solid-state NMR data.
Related Articles Structure of gramicidin a in a lipid bilayer environment determined using molecular dynamics simulations and solid-state NMR data.
J Am Chem Soc. 2003 Aug 13;125(32):9868-77
Authors: Allen TW, Andersen OS, Roux B
Two different high-resolution structures recently have been proposed for the membrane-spanning gramicidin A channel: one based on solid-state NMR experiments in oriented phospholipid...
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11-24-2010 09:16 PM
[NMR paper] High-resolution NMR structure of the chemically-synthesized melanocortin receptor bin
High-resolution NMR structure of the chemically-synthesized melanocortin receptor binding domain AGRP(87-132) of the agouti-related protein.
Related Articles High-resolution NMR structure of the chemically-synthesized melanocortin receptor binding domain AGRP(87-132) of the agouti-related protein.
Biochemistry. 2001 Dec 25;40(51):15520-7
Authors: McNulty JC, Thompson DA, Bolin KA, Wilken J, Barsh GS, Millhauser GL
The agouti-related protein (AGRP) is an endogenous antagonist of the melanocortin receptors MC3R and MC4R found in the hypothalamus...
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11-19-2010 08:44 PM
[NMR paper] A high-resolution 1H NMR approach for structure determination of membrane peptides an
A high-resolution 1H NMR approach for structure determination of membrane peptides and proteins in non-deuterated detergent: application to mastoparan X solubilized in n-octylglucoside.
Related Articles A high-resolution 1H NMR approach for structure determination of membrane peptides and proteins in non-deuterated detergent: application to mastoparan X solubilized in n-octylglucoside.
J Biomol NMR. 1995 Jun;5(4):345-52
Authors: Seigneuret M, Lévy D
Application of 1H 2D NMR methods to solubilized membrane proteins and peptides has up to now...
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[NMR paper] High-resolution structure of the phosphorylated form of the histidine-containing phos
High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE data.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE data.
J Mol Biol. 1995 Feb 10;246(1):180-93
Authors: van...
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[NMR paper] High-resolution structure of the oligomerization domain of p53 by multidimensional NM
High-resolution structure of the oligomerization domain of p53 by multidimensional NMR.
Related Articles High-resolution structure of the oligomerization domain of p53 by multidimensional NMR.
Science. 1994 Jul 15;265(5170):386-91
Authors: Clore GM, Omichinski JG, Sakaguchi K, Zambrano N, Sakamoto H, Appella E, Gronenborn AM
The three-dimensional structure of the oligomerization domain (residues 319 to 360) of the tumor suppressor p53 has been solved by multidimensional heteronuclear magnetic resonance (NMR) spectroscopy. The domain forms a...
High-resolution polypeptide structure in a lamellar phase lipid environment from soli
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