Related ArticlesNMR studies of the major coat protein of bacteriophage M13. Structural information of gVIIIp in dodecylphosphocholine micelles.
Eur J Biochem. 1995 Sep 1;232(2):490-500
Authors: Papavoine CH, Aelen JM, Konings RN, Hilbers CW, Van de Ven FJ
The membrane-bound form of the major coat protein (gVIIIp) of bacteriophage M13 has been studied using nuclear magnetic resonance spectroscopy. As membrane mimetics, we used dodecylphosphocholine (DodPCho) detergent micelles to solubilize the protein. We were able to nearly completely assign all resonances of the protein solubilized in DodPCho micelles by using both homonuclear and heteronuclear multidimensional experiments. Based on the patterns of the nuclear Overhauser enhancements and the chemical shifts of the resonances, we deduced the secondary structure of the protein. Additional structural information was obtained from amide proton exchange data and J-coupling constants. The protein consists of two alpha-helices which are connected by a hinge region around residue 21. From spin-label experiments, the location of the protein relative to the DodPCho micelles was determined. One, hydrophobic, helix spans the micelle, and another, amphipathic, helix, is located beneath the surface of the micelle. Comparison of the data of gVIIIp in DodPCho micelles with those of gVIIIp in sodium dodecyl sulfate (SDS) micelles [Van de Ven, F. J. M., van Os, J. W. M., Aelen, J. M. A., Wymenga, S. S., Remerowski, M. L., Konings, R. N. H. & Hilbers, C. W. (1993) Biochemistry 32, 8322-8328; Papavoine, C. H. M., Konings, R. N. H., Hilbers, C. W. & Van de Ven, F. J. M. (1994) Biochemistry 33, 12,990-12,997] reveals that the structures of the protein in the two detergent micelles are very similar. They differ only in the arrangement of the detergent molecules around the protein. For gVIIIp in SDS micelles, we found a micellar structure which is distorted near the C-terminus of the protein; whereas for DodPCho micelles, both distorted and regular elliptical micelles occur. This distortion is probably due to the interaction of the positively charged lysine side chains with the negatively charged head group of the detergent molecules.
Long-Term-Stable Ether-Lipid vs Conventional Ester-Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides.
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J Phys Chem B. 2011 Feb 10;
Authors: Bertelsen K, Vad B, Nielsen EH, Hansen SK, Skrydstrup T, Otzen DE, Vosegaard T, Nielsen NC
Recently, ether lipids have been introduced as long-term stable alternatives to the more natural,...
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[NMR paper] NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor.
NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor.
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Structure. 2005 Aug;13(8):1193-202
Authors: Arolas JL, D'Silva L, Popowicz GM, Aviles FX, Holak TA, Ventura S
The III-A intermediate constitutes the major rate-determining step in the oxidative folding of leech carboxypeptidase inhibitor...
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(31)P NMR and AFM studies on the destabilization of cell and model membranes by the major bovine seminal plasma protein, PDC-109.
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IUBMB Life. 2010 Nov;62(11):841-51
Authors: Damai RS, Sankhala RS, Anbazhagan V, Swamy MJ
The effect of PDC-109 binding to dimyristoylphosphatidylcholine (DMPC) and dipalmitoylphosphatidylglycerol (DPPG) multilamellar vesicles (MLVs) and supported membranes was investigated by...
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[NMR paper] Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spec
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J Mol Biol. 2004 Aug 13;341(3):869-79
Authors: Thiriot DS, Nevzorov AA, Zagyanskiy L, Wu CH, Opella SJ
The atomic resolution structure of Pf1 coat protein determined by solid-state NMR spectroscopy of magnetically aligned filamentous bacteriophage particles in solution is compared to the structures previously determined by X-ray fiber and...
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[NMR paper] Structure of the coat protein in fd filamentous bacteriophage particles determined by
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Proc Natl Acad Sci U S A. 2003 May 27;100(11):6458-63
Authors: Zeri AC, Mesleh MF, Nevzorov AA, Opella SJ
The atomic resolution structure of fd coat protein determined by solid-state NMR spectroscopy of magnetically aligned filamentous bacteriophage particles differs from that previously determined...
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[NMR paper] Structural and orientational information of the membrane embedded M13 coat protein by
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Biochim Biophys Acta. 2000 Jan 15;1463(1):151-61
Authors: Glaubitz C, Gröbner G, Watts A
Oriented and unoriented M13 coat protein, incorporated into dimyristoyl phosphatidylcholine bilayers, has been studied by (13)C-magic angle spinning nuclear magnetic resonance (MAS NMR) spectroscopy. Rotational...
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[NMR paper] Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by sol
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by solution NMR.
Biochemistry. 1996 Apr 23;35(16):5145-57
Authors: Williams KA, Farrow NA, Deber CM, Kay LE
The structure and dynamics of the 53-residue filamentous bacteriophage IKe major coat protein in fully protonated myristoyllysophosphatidylglycerol (MPG)...
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[NMR paper] NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat pr
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Science. 1991 May 31;252(5010):1303-5
Authors: Shon KJ, Kim Y, Colnago LA, Opella SJ
Filamentous bacteriophage coat protein undergoes a remarkable structural transition during the viral assembly process as it is transferred from the membrane environment of the cell, where it spans the phospholipid bilayer, to the newly extruded virus particles....
NMR studies of the major coat protein of bacteriophage M13. Structural information of
Linear Mode
