NMR study of the structure and self-association of Core peptide in aqueous solution and DPC micelles.
Biopolymers. 2011;96(2):177-80
Authors: Zheng G, Torres AM, Ali M, Manolios N, Price WS
Core peptide is a hydrophobic peptide derived from the T-cell antigen receptor-alpha chain (TCR-alpha) transmembrane region with therapeutic potential. The mechanism by which the peptide inserts into the membrane, including any requirements to change conformational or association states during the insertion, is unclear. Here, the self-association and secondary structure of Core peptide in aqueous solution and in dodecylphosphocholine (DPC) micelles were examined using various nuclear magnetic resonance (NMR) techniques. NMR diffusion measurements were performed on 0.05, 1, and 5 mM Core peptide in D2O. These samples had pH values varying from 3 to 4. A constant measured diffusion coefficient of 2 X 10(-10) m2 s(-1) was observed in these samples indicating that Core peptide was monomeric. Multidimensional NMR experiments (i.e., TOCSY and NOESY) revealed the formation of beta-strands in water at low pH and random coil in DPC micelles. The results of this study reveal that at relatively low pH, the insertion mechanism must involve Core peptide in the monomeric state but it undergoes a conformational transition during membrane insertion.
[NMR paper] NMR study of a membrane protein in detergent-free aqueous solution.
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Proc Natl Acad Sci U S A. 2005 Jun 21;102(25):8893-8
Authors: Zoonens M, Catoire LJ, Giusti F, Popot JL
One of the major obstacles to membrane protein (MP) structural studies is the destabilizing effect of detergents. Amphipols (APols) are short amphipathic polymers that can substitute for detergents to keep MPs water-soluble under mild conditions. In the present work, we have explored the...
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[NMR paper] Study of the behaviour of amino acids in aqueous solution by time-domain NMR and high
Study of the behaviour of amino acids in aqueous solution by time-domain NMR and high-resolution NMR.
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Magn Reson Chem. 2005 Apr;43(4):309-15
Authors: Khallouk M, Rutledge DN, Silva AM, Delgadillo I
The study of protein hydration by time-domain NMR is complicated by the great number of interactions involved, resulting from the presence of several amino acids and the possible modifications produced by the various structures....
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NMR structure note: solution structure of the core domain of MESD that is essential f
NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6.
J Biomol NMR. 2010 Aug;47(4):283-8
Authors: Chen J, Li Q, Liu CC, Zhou B, Bu G, Wang J
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[NMR paper] PhoE signal peptide inserts into micelles as a dynamic helix-break-helix structure, w
PhoE signal peptide inserts into micelles as a dynamic helix-break-helix structure, which is modulated by the environment. A two-dimensional 1H NMR study.
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Biochemistry. 1995 Sep 12;34(36):11617-24
Authors: Chupin V, Killian JA, Breg J, de Jongh HH, Boelens R, Kaptein R, de Kruijff B
Proteins that are destined for export out of the cytoplasm of Escherichia coli cells are...
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[NMR paper] The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution.
The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution.
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Biochemistry. 1991 Jul 2;30(26):6563-74
Authors: Weber C, Wider G, von Freyberg B, Traber R, Braun W, Widmer H, Wüthrich K
Cyclosporin A bound to the presumed receptor protein cyclophilin was studied in aqueous solution at pH 6.0 by nuclear magnetic resonance spectroscopy using uniform 15N- or 13C-labeling of cyclosporin A and heteronuclear spectral editing techniques....
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NMR structure note: solution structure of the core domain of MESD that is essential f
NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6
Content Type Journal Article
DOI 10.1007/s10858-010-9426-8
Authors
Jianglei Chen, Wayne State University Department of Biochemistry and Molecular Biology, School of Medicine Detroit MI 48201 USA
Qianqian Li, Wayne State University Department of Biochemistry and Molecular Biology, School of Medicine Detroit MI 48201 USA
Chia-Chen Liu, Washington University Departments of Pediatrics, and Cell Biology and Physiology, School of Medicine St. Louis MO 63110 USA
NMR study of the structure and self-association of Core peptide in aqueous solution and DPC micelles.
Linear Mode
