Related ArticlesTwo-dimensional 1H NMR study of recombinant insect defensin A in water: resonance assignments, secondary structure and global folding.
J Biomol NMR. 1992 May;2(3):235-56
Authors: Bonmatin JM, Bonnat JL, Gallet X, Vovelle F, Ptak M, Reichhart JM, Hoffmann JA, Keppi E, Legrain M, Achstetter T
A 500 MHz 2D 1H NMR study of recombinant insect defensin A is reported. This defense protein of 40 residues contains 3 disulfide bridges, is positively charged and exhibits antibacterial properties. 2D NMR maps of recombinant defensin A were fully assigned and secondary structure elements were localized. The set of NOE connectivities, 3JNH-alpha H coupling constants as well as 1H/2H exchange rates and delta delta/delta T temperature coefficients of NH protons strongly support the existence of an alpha-helix (residues 14-24) and of an antiparallel beta-sheet (residues 27-40). Models of the backbone folding were generated by using the DISMAN program and energy refined by using the AMBER program. This was done on the basis of: (i) 133 selected NOEs, (ii) 21 dihedral restraints from 3JNH-alpha H coupling constants, (iii) 12 hydrogen bonds mostly deduced from 1H/2H exchange rates or temperature coefficients, in addition to 9 initial disulfide bridge covalent constraints. The two secondary structure elements and the two bends connecting them involve approximately 70% of the total number of residues, which impose some stability in the C-terminal part of the molecule. The remaining N-terminal fragment forms a less well defined loop. This spatial organization, in which a beta-sheet is linked to an alpha-helix by two disulfide bridges and to a large loop by a third disulfide bridge, is rather similar to that found in scorpion charybdotoxin and seems to be partly present in several invertebrate toxins.
The insect defensin lucifensin from Lucilia sericata
The insect defensin lucifensin from Lucilia sericata
The insect defensin lucifensin from Lucilia sericata
Content Type Journal Article
Category NMR structure note
Pages 1-6
DOI 10.1007/s10858-012-9608-7
[NMR paper] Solution structure of Pisum sativum defensin 1 by high resolution NMR: plant defensin
Solution structure of Pisum sativum defensin 1 by high resolution NMR: plant defensins, identical backbone with different mechanisms of action.
Related Articles Solution structure of Pisum sativum defensin 1 by high resolution NMR: plant defensins, identical backbone with different mechanisms of action.
J Mol Biol. 2002 Jan 25;315(4):749-57
Authors: Almeida MS, Cabral KM, Kurtenbach E, Almeida FC, Valente AP
Pisum sativum defensin 1 (Psd1) is a 46 amino acid residue plant defensin isolated from seeds of pea. The three-dimensional structure in...
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[NMR paper] Probing internal water molecules in proteins using two-dimensional 19F-1H NMR.
Probing internal water molecules in proteins using two-dimensional 19F-1H NMR.
Related Articles Probing internal water molecules in proteins using two-dimensional 19F-1H NMR.
J Biomol NMR. 1995 Jun;5(4):415-9
Authors: Cistola DP, Hall KB
A simple approach for detecting internal water molecules in proteins in solution is described. This approach combines 19F-detected heteronuclear Overhauser and exchange spectroscopy (HOESY) with site-specific 19F substitution. The model system employed was intestinal fatty acid-binding protein complexed with...
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[NMR paper] NMR study of collagen-water interactions.
NMR study of collagen-water interactions.
Related Articles NMR study of collagen-water interactions.
Biopolymers. 1994 Dec;34(12):1615-26
Authors: Renou JP, Bonnet M, Bielicki G, Rochdi A, Gatellier P
A proton magnetic resonance study of different cross-linked collagens was performed as a function of water content and temperature. Collagens from three connective tissues (calf, steer, and cow) were chosen according to the different number of nonreducible multivalent cross-links, which increases during the life of animal. Samples were hydrated...
Two-dimensional 1H NMR study of recombinant insect defensin A in water: resonance ass
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