Related ArticlesInvestigating 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 charged. The conformational coupling between the transmembrane span and the cytoplasmic domain of PMP1 was investigated from 1H-nuclear magnetic resonance data of two synthetic fragments: F9-F38, i.e. 80% of the whole sequence, and Y25-F38, the isolated cytoplasmic domain. Highly disordered in aqueous solution, the Y25-F38 peptide adopts a well-defined conformation in the presence of dodecylphosphocholine micelles. Compared with the long PMP1 fragment, this structure exhibits both native and non-native elements. Our results make it possible to assess the influence of a hydrophobic anchor on the intrinsic conformational propensity of a cytoplasmic domain.
Site-Specific Solid-State NMR Detection of Hydrogen-Deuterium Exchange Reveals Conformational Changes in a 7-Helical Transmembrane Protein.
Site-Specific Solid-State NMR Detection of Hydrogen-Deuterium Exchange Reveals Conformational Changes in a 7-Helical Transmembrane Protein.
Site-Specific Solid-State NMR Detection of Hydrogen-Deuterium Exchange Reveals Conformational Changes in a 7-Helical Transmembrane Protein.
Biophys J. 2011 Aug 3;101(3):L23-L25
Authors: Wang S, Shi L, Kawamura I, Brown LS, Ladizhansky V
Solid-state NMR spectroscopy is an efficient tool for following conformational dynamics of membrane proteins at atomic resolution. We used this technique for the site-specific...
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08-03-2011 12:00 PM
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Protein Expr Purif. 2011 Feb 11;
Authors: Wang X, Gill Jr RL, Zhu Q, Tian F
LR11 (SorLA) is a recently identified neuronal protein that interacts with amyloid precursor protein (APP), a central player...
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02-16-2011 07:40 PM
[NMR paper] Conformational heterogeneity of transmembrane residues after the Schiff base reproton
Conformational heterogeneity of transmembrane residues after the Schiff base reprotonation of bacteriorhodopsin: 15N CPMAS NMR of D85N/T170C membranes.
Related Articles Conformational heterogeneity of transmembrane residues after the Schiff base reprotonation of bacteriorhodopsin: 15N CPMAS NMR of D85N/T170C membranes.
FEBS J. 2005 May;272(9):2152-64
Authors: Mason AJ, Turner GJ, Glaubitz C
bR, N-like and O-like intermediate states of methionine-labelled wild type and D85N/T170C bacteriorhodopsin were accumulated in native membranes by...
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11-25-2010 08:21 PM
[NMR paper] Investigating the dynamic properties of the transmembrane segment of phospholamban in
Investigating the dynamic properties of the transmembrane segment of phospholamban incorporated into phospholipid bilayers utilizing 2H and 15N solid-state NMR spectroscopy.
Related Articles Investigating the dynamic properties of the transmembrane segment of phospholamban incorporated into phospholipid bilayers utilizing 2H and 15N solid-state NMR spectroscopy.
Biochemistry. 2004 Nov 9;43(44):13899-909
Authors: Tiburu EK, Karp ES, Dave PC, Damodaran K, Lorigan GA
(2)H and (15)N solid-state NMR spectroscopic techniques were used to investigate...
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11-24-2010 10:03 PM
[NMR paper] Characterization of the monomeric form of the transmembrane and cytoplasmic domains o
Characterization of the monomeric form of the transmembrane and cytoplasmic domains of the integrin beta 3 subunit by NMR spectroscopy.
Related Articles Characterization of the monomeric form of the transmembrane and cytoplasmic domains of the integrin beta 3 subunit by NMR spectroscopy.
Biochemistry. 2002 Dec 31;41(52):15618-24
Authors: Li R, Babu CR, Valentine K, Lear JD, Wand AJ, Bennett JS, DeGrado WF
We have characterized a membrane protein containing residues P688-T762 of the integrin beta3 subunit, encompassing its transmembrane and...
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11-24-2010 08:58 PM
[NMR paper] The cytoplasmic helix of cannabinoid receptor CB2, a conformational study by circular
The cytoplasmic helix of cannabinoid receptor CB2, a conformational study by circular dichroism and (1)H NMR spectroscopy in aqueous and membrane-like environments.
Related Articles The cytoplasmic helix of cannabinoid receptor CB2, a conformational study by circular dichroism and (1)H NMR spectroscopy in aqueous and membrane-like environments.
J Pept Res. 2002 Sep;60(3):169-77
Authors: Choi G, Landin J, Xie XQ
The cytoplasmic helix domain (fourth cytoplasmic loop, helix 8) of numerous G protein-coupled receptors (GPCRs) such as rhodopsin and...
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Conformational dependence of 13C shielding and coupling constants for methionine
Abstract Methionine residues fulfill a broad range of roles in protein function related to conformational plasticity, ligand binding, and sensing/mediating the effects of oxidative stress. A high degree of internal mobility, intrinsic detection sensitivity of the methyl group, and low copy number have made methionine labeling a popular approach for NMR investigation of selectively labeled protein macromolecules. However, selective labeling approaches are subject to more limited information content. In order to optimize the information available from such studies, we have performed DFT...
Investigating the conformational coupling between the transmembrane and cytoplasmic d
Linear Mode
