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NMR processing:
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Side-chains:
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Ab initio:
GeNMR
Cyana
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Fragment-based:
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Refinement:
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Fragment-based:
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Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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Interactions from chemical shifts:
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Methyl S2
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Molecular dynamics:
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From structure:
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ArShift- Aromatic
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PPM
CheShift-2- Cα
From sequence:
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Camcoil
Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
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NMR sample preparation:
Protein disorder:
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Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
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Solid-state NMR:
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Default CD and NMR structural characterization of ceratotoxins, natural peptides with antimic

CD and NMR structural characterization of ceratotoxins, natural peptides with antimicrobial activity.

Related Articles CD and NMR structural characterization of ceratotoxins, natural peptides with antimicrobial activity.

Biopolymers. 1996 Nov;39(5):653-64

Authors: Ragona L, Molinari H, Zetta L, Longhi R, Marchini D, Dallai R, Bernini LF, Lozzi L, Scarselli M, Niccolai N

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.

PMID: 8875820 [PubMed - indexed for MEDLINE]



Source: PubMed
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