Helix conformation of a small peptide melittin in a methanol-water mixed solvent studied by NMR.
Protein Pept Lett. 2011 Mar;18(3):318-26
Authors: Miura Y
Temperature dependence of the ?-helix conformation of bee venom melittin in methanol-water mixed solvents has been examined by NMR, in order to elucidate conformation stability and a phase diagram. At high methanol concentration of 100 - ca. 80 wt.%, melittin forms a full ?-helix conformation in the temperature range from 25 °C to 60 °C. At intermediate methanol concentration of ca. 80 - ca. 25 wt.%, it undergoes a thermal transformation from a full ?-helix to a partial ?-helix. In solutions of low methanol concentrations of ca. 25 - 0 wt.%, partial ?-helix monomers and their self-aggregated conformers coexist at low temperatures, and the relative number of the monomers increases with increase in temperature. The monomers turn to a random coil state at high temperatures only below ca. 10 wt. % methanol concentrations. The thermal transitions are discussed from the viewpoint of stability of intra-molecular hydrogen bonds and inter-molecular hydrophobic interactions.
[NMR paper] NMR structural analysis of a peptide mimic of the bridging sheet of HIV-1 gp120 in methanol and water.
NMR structural analysis of a peptide mimic of the bridging sheet of HIV-1 gp120 in methanol and water.
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Biochem J. 2005 Sep 1;390(Pt 2):573-81
Authors: Chakraborty K, Shivakumar P, Raghothama S, Varadarajan R
gp120 is a subunit of the Env (viral envelope protein) of HIV-1. The protein consists of inner and outer domains linked by a bridging sheet. Several gp120 residues that bind the neutralizing antibody 17b as well as the...
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[NMR paper] The conformation of the cytoplasmic helix 8 of the CB1 cannabinoid receptor using NMR
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Biochim Biophys Acta. 2005 Feb 1;1668(1):1-9
Authors: Choi G, Guo J, Makriyannis A
The cytoplasmic helix domain (fourth cytoplasmic loop, helix 8) of numerous GPCRs such as rhodopsin and the beta-adrenergic receptor exhibits unique structural and functional characteristics. Computational models also predict the...
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[NMR paper] Membrane protein-lipid interactions in mixed micelles studied by NMR spectroscopy wit
Membrane protein-lipid interactions in mixed micelles studied by NMR spectroscopy with the use of paramagnetic reagents.
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Chembiochem. 2004 Apr 2;5(4):467-73
Authors: Hilty C, Wider G, Fernández C, Wüthrich K
For solution NMR studies of the structure and function of membrane proteins, these macromolecules have to be reconstituted and solubilized in detergent micelles. Detailed characterization of the mixed...
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11-24-2010 09:51 PM
[NMR paper] Dynamics of a de novo designed three-helix bundle protein studied by 15N, 13C, and 2H
Dynamics of a de novo designed three-helix bundle protein studied by 15N, 13C, and 2H NMR relaxation methods.
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Biochemistry. 2001 Aug 14;40(32):9560-9
Authors: Walsh ST, Lee AL, DeGrado WF, Wand AJ
Understanding how the amino acid sequence of a polypeptide chain specifies a unique, functional three-dimensional structure remains an important goal, especially in the context of the emerging discipline of de novo protein...
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11-19-2010 08:44 PM
[NMR paper] Pressure-dependent changes in the structure of the melittin alpha-helix determined by
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J Biomol NMR. 2001 Feb;19(2):115-24
Authors: Iwadate M, Asakura T, Dubovskii PV, Yamada H, Akasaka K, Williamson MP
A novel method is described, which uses changes in NMR chemical shifts to characterise the structural change in a protein with pressure. Melittin in methanol is a small alpha-helical protein, and its chemical shifts change linearly...
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11-19-2010 08:32 PM
[NMR paper] PhoE signal peptide inserts into micelles as a dynamic helix-break-helix structure, w
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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 influence of hydration on the conformation of bovine serum albumin studied by sol
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Biopolymers. 1993 Dec;33(12):1871-6
Authors: Gregory RB, Gangoda M, Gilpin RK, Su W
13C proton-decoupled cross-polarization magic-angle spinning nmr spectra of bovine serum albumin are reported as a function of hydration. Increases in hydration level enhance the resolution of the peak centered at...
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[NMR paper] The influence of hydration on the conformation of lysozyme studied by solid-state 13C
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Biopolymers. 1993 Apr;33(4):513-9
Authors: Gregory RB, Gangoda M, Gilpin RK, Su W
13C proton decoupled cross-polarization magic-angle spinning nmr spectra of lysozyme are reported as a function of hydration. Increases in hydration level enhance the resolution of the spectra, particularly in the aliphatic region, but has no...
Helix conformation of a small peptide melittin in a methanol-water mixed solvent studied by NMR.
Linear Mode
