Antibacterial properties of the secretion from the female reproductive accessory glands of medfly Ceratitis capitata are mostly ascribed to the presence of two peptides, ceratotoxin A and B, which exhibit a strong activity against gram-positive and gram-negative bacterial strains, and show sequence and function homology with cecropins, melittin, and magainins. CD experiments performed in different solvents indicate the presence of a significant content of helical structures in organic solvent. Two-dimensional nmr results for ceratotoxin A in methanol show a helical behavior for the 8-25 region of the peptide. A ramachandran classification of each residue for the structures obtained from distance geometry calculations lead to the definition of four structural families in which the central segment 10-19 is always helical and differences refer to residues 8-9 and 19-23. A sequence analysis of the two ceratotoxins and a systematic search on the protein data bank revealed the occurrence of a KX-hydrophobic-hydrophobic-P motif that seems to be important for helix stabilization.
Solution and Solid-State NMR Structural Studies of Antimicrobial Peptides LPcin-I and LPcin-II.
Solution and Solid-State NMR Structural Studies of Antimicrobial Peptides LPcin-I and LPcin-II.
Solution and Solid-State NMR Structural Studies of Antimicrobial Peptides LPcin-I and LPcin-II.
Biophys J. 2011 Sep 7;101(5):1193-201
Authors: Park TJ, Kim JS, Ahn HC, Kim Y
Abstract
Lactophoricin (LPcin-I) is an antimicrobial, amphiphatic, cationic peptide with 23-amino acid residues isolated from bovine milk. Its analogous peptide, LPcin-II, lacks six N-terminal amino acids compared to LPcin-I. Interestingly, LPcin-II does not display any...
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Long-Term-Stable Ether-Lipid vs Conventional Ester-Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides.
Long-Term-Stable Ether-Lipid vs Conventional Ester-Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides.
Long-Term-Stable Ether-Lipid vs Conventional Ester-Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides.
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] Structural analysis of Bombyx mori silk fibroin peptides with formic acid treatment u
Structural analysis of Bombyx mori silk fibroin peptides with formic acid treatment using high-resolution solid-state 13C NMR spectroscopy.
Related Articles Structural analysis of Bombyx mori silk fibroin peptides with formic acid treatment using high-resolution solid-state 13C NMR spectroscopy.
Biomacromolecules. 2004 Sep-Oct;5(5):1763-9
Authors: Yao J, Ohgo K, Sugino R, Kishore R, Asakura T
Bombyx mori silk fibroin fiber is a fibrous protein produced by the silkworm at room temperature and from an aqueous solution whose primary structure is...
[NMR paper] NMR structural characterization of the CDK inhibitor p19INK4d.
NMR structural characterization of the CDK inhibitor p19INK4d.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR structural characterization of the CDK inhibitor p19INK4d.
FEBS Lett. 1997 Jan 20;401(2-3):127-32
Authors: Kalus W, Baumgartner R, Renner C, Noegel A, Chan FK, Winoto A, Holak TA
p19INK4d is a 165 amino acid protein that belongs to the INK4 family of CDK4 and CDK6 inhibitors. Assignments of 1H, 15N and 13C resonances have enabled the determination of the...
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[NMR paper] Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization o
Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization of helicity in the H1 peptides by NMR.
Related Articles Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization of helicity in the H1 peptides by NMR.
J Biol Chem. 1994 Jan 21;269(3):1785-93
Authors: Draeger LJ, Mullen GP
The carboxyl-terminal 92 residues of c-Myc-92 display site-specific DNA binding specificity for the consensus sequence 5'-CACCACGTGGTG-3' (Blackwell, T. K., Kretzner, L., Blackwood, E. M., Eisenman, R. N., and...
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[NMR paper] Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization o
Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization of helicity in the H1 peptides by NMR.
Related Articles Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization of helicity in the H1 peptides by NMR.
J Biol Chem. 1994 Jan 21;269(3):1785-93
Authors: Draeger LJ, Mullen GP
The carboxyl-terminal 92 residues of c-Myc-92 display site-specific DNA binding specificity for the consensus sequence 5'-CACCACGTGGTG-3' (Blackwell, T. K., Kretzner, L., Blackwood, E. M., Eisenman, R. N., and...
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Precise structural determination of weakly binding peptides by utilizing dihedral ang
Abstract Structural determination of target-bound conformations of peptides is of primary importance for the optimization of peptide ligands and peptideā??mimetic design. In the structural determination of weakly binding ligands, transferred nuclear Overhauser effect (TrNOE) methods have been widely used. However, not many distance constraints can be obtained from small peptide ligands by TrNOE, especially for peptides bound to a target molecule in an extended conformation. Therefore, for precise structural determination of weakly binding peptides, additional structural constraints are...
CD and NMR structural characterization of ceratotoxins, natural peptides with antimic
Linear Mode
