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 and reversibly with pressure between 1 and 2000 bar. An improved relationship between structure and HN shift has been calculated, and used to drive a molecular dynamics-based calculation of the change in structure. With pressure, the helix is compressed, with the H-O distance of the NH-O=C hydrogen bonds decreased by 0.021 +/- 0.039 A, leading to an overall compression along the entire helix of about 0.4 A, corresponding to a static compressibility of 6 x 10(-6) bar(-1). The backbone dihedral angles phi and psi are altered by no more than +/- 3 degrees for most residues with a negative correlation coefficient of -0.85 between phi(i) and psi(i - 1), indicating that the local conformation alters to maintain hydrogen bonds in good geometries. The method is shown to be capable of calculating structural change with high precision, and the results agree with structural changes determined using other methodologies.
Helix conformation of a small peptide melittin in a methanol-water mixed solvent studied by NMR.
Helix conformation of a small peptide melittin in a methanol-water mixed solvent studied by NMR.
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...
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[NMR paper] The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR
The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy.
Biochemistry. 1997 Nov 4;36(44):13657-66
Authors: Wang G, Sparrow JT, Cushley RJ
The conformation of a synthetic peptide of 46 residues from apoA-I was investigated by fluorescence, CD, and 2D NMR spectroscopies in lipid-mimetic environments....
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[NMR paper] Proline pipe helix: structure of the tus proline repeat determined by 1H NMR.
Proline pipe helix: structure of the tus proline repeat determined by 1H NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Proline pipe helix: structure of the tus proline repeat determined by 1H NMR.
Biochemistry. 1996 Jan 23;35(3):698-703
Authors: Butcher DJ, Nedved ML, Neiss TG, Moe GR
The structure of a 22 amino acid peptide, TPPI , that is similar to the proline repeat segment of the replication arrest protein, Tus, has been determined by 1H NMR in 50% trifluroethanol. The...
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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.
Related Articles 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.
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] Solution structure of human type-alpha transforming growth factor determined by heter
Solution structure of human type-alpha transforming growth factor determined by heteronuclear NMR spectroscopy and refined by energy minimization with restraints.
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Biochemistry. 1993 Jul 27;32(29):7334-53
Authors: Moy FJ, Li YC, Rauenbuehler P, Winkler ME, Scheraga HA, Montelione GT
Human type-alpha transforming growth factor (hTGF alpha) is a small mitogenic protein...
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[NMR paper] Secondary structure of the homeo domain of yeast alpha 2 repressor determined by NMR
Secondary structure of the homeo domain of yeast alpha 2 repressor determined by NMR spectroscopy.
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Genes Dev. 1991 May;5(5):764-72
Authors: Phillips CL, Vershon AK, Johnson AD, Dahlquist FW
The yeast alpha 2 protein is a regulator of cell type in Saccharomyces cerevisiae. It represses transcription of a set of target genes by binding to an operator located upstream of each of these genes. The alpha 2 protein shares weak sequence...
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[NMR paper] Probing the relationship between alpha-helix formation and calcium affinity in tropon
Probing the relationship between alpha-helix formation and calcium affinity in troponin C: 1H NMR studies of calcium binding to synthetic and variant site III helix-loop-helix peptides.
Related Articles Probing the relationship between alpha-helix formation and calcium affinity in troponin C: 1H NMR studies of calcium binding to synthetic and variant site III helix-loop-helix peptides.
Biochemistry. 1991 Aug 27;30(34):8339-47
Authors: Shaw GS, Hodges RS, Sykes BD
Three 34-residue peptides corresponding to the high-affinity calcium-binding site...
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[NMR paper] Probing the relationship between alpha-helix formation and calcium affinity in tropon
Probing the relationship between alpha-helix formation and calcium affinity in troponin C: 1H NMR studies of calcium binding to synthetic and variant site III helix-loop-helix peptides.
Related Articles Probing the relationship between alpha-helix formation and calcium affinity in troponin C: 1H NMR studies of calcium binding to synthetic and variant site III helix-loop-helix peptides.
Biochemistry. 1991 Aug 27;30(34):8339-47
Authors: Shaw GS, Hodges RS, Sykes BD
Three 34-residue peptides corresponding to the high-affinity calcium-binding site...
Pressure-dependent changes in the structure of the melittin alpha-helix determined by
Linear Mode
