Related Articles1H-NMR-derived secondary structure and overall fold of a natural anatoxin from the scorpion Androctonus australis hector.
Eur J Biochem. 1997 Aug 1;247(3):1118-26
Authors: Blanc E, Hassani O, Meunier S, Mansuelle P, Sampieri F, Rochat H, Darbon H
The venom of the scorpion Androctonus australis hector contains several protein neurotoxins of which structure and structure/activity relationships have been extensively studied. It also contains polypeptides such as Aah STR1, which are not toxic, while having highly similar sequences to fully active toxins. We have determined the solution structure of Aah STR1 by use of conventional two-dimensional NMR techniques followed by distance-geometry and energy minimization. We have demonstrated that, despite its lack of toxicity, Aah STR1 is structurally highly related to anti-mammal scorpion toxins specific for Na+ channels. The calculated structure is composed of a short alpha-helix (residues 26-33) connected by a tight turn to a three-stranded antiparallel beta-sheet (sequences 3-6, 38-41 and 44-48). This beta-sheet is right-handed twisted as usual for such secondary structures. The beta-turn connecting the strands 38-41 and 44-48 belongs to type II'. The overall fold of Aah STR1 is typical of beta-type scorpion toxins. This is, however, the first example of such a fold in Old World scorpion toxins. Either the absence of a basic residue in position 63 or the high mobility of loops, compared to active beta-type neurotoxins, may explain the lack of activity of this protein.
VITAL NMR: using chemical shift derived secondary structure information for a limited set of amino acids to assess homology model accuracy
VITAL NMR: using chemical shift derived secondary structure information for a limited set of amino acids to assess homology model accuracy
Abstract Homology modeling is a powerful tool for predicting protein structures, whose success depends on obtaining a reasonable alignment between a given structural template and the protein sequence being analyzed. In order to leverage greater predictive power for proteins with few structural templates, we have developed a method to rank homology models based upon their compliance to secondary structure derived from experimental solid-state NMR...
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[NMR paper] NMR assignments, secondary structure, and global fold of calerythrin, an EF-hand calc
NMR assignments, secondary structure, and global fold of calerythrin, an EF-hand calcium-binding protein from Saccharopolyspora erythraea.
Related Articles NMR assignments, secondary structure, and global fold of calerythrin, an EF-hand calcium-binding protein from Saccharopolyspora erythraea.
Protein Sci. 1999 Dec;8(12):2580-8
Authors: Aitio H, Annila A, Heikkinen S, Thulin E, Drakenberg T, Kilpeläinen I
Calerythrin is a 20 kDa calcium-binding protein isolated from gram-positive bacterium Saccharopolyspora erythraea. Based on amino acid...
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[NMR paper] 1H-NMR-derived secondary structure and the overall fold of the potent anti-mammal and
1H-NMR-derived secondary structure and the overall fold of the potent anti-mammal and anti-insect toxin III from the scorpion Leiurus quinquestriatus quinquestriatus.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H-NMR-derived secondary structure and the overall fold of the potent anti-mammal and anti-insect toxin III from the scorpion Leiurus quinquestriatus quinquestriatus.
Eur J Biochem. 1996 Mar 1;236(2):395-404
Authors: Landon C,...
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[NMR paper] Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein u
Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein using three- and four-dimensional heteronuclear (13C,15N) NMR spectroscopy.
Related Articles Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein using three- and four-dimensional heteronuclear (13C,15N) NMR spectroscopy.
Biochemistry. 1994 Sep 6;33(35):10731-42
Authors: Moy FJ, Lowry DF, Matsumura P, Dahlquist FW, Krywko JE, Domaille PJ
NMR spectroscopy has been used to study recombinant Escherichia coli CheY, a 128-residue...
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[NMR paper] 1H-NMR resonance assignments, secondary structure, and global fold of the TR1C fragme
1H-NMR resonance assignments, secondary structure, and global fold of the TR1C fragment of turkey skeletal troponin C in the calcium-free state.
Related Articles 1H-NMR resonance assignments, secondary structure, and global fold of the TR1C fragment of turkey skeletal troponin C in the calcium-free state.
Biochemistry. 1993 Apr 6;32(13):3461-7
Authors: Findlay WA, Sykes BD
The TR1C fragment of turkey skeletal muscle TnC (residues 12-87) comprises the two regulatory calcium binding sites of the protein. Complete assignments of the 1H-NMR...
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[NMR paper] Secondary structure of human granulocyte colony-stimulating factor derived from NMR s
Secondary structure of human granulocyte colony-stimulating factor derived from NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Secondary structure of human granulocyte colony-stimulating factor derived from NMR spectroscopy.
FEBS Lett. 1992 Dec 21;314(3):435-9
Authors: Zink T, Ross A, Ambrosius D, Rudolph R, Holak TA
Recombinant 15N-, 13C-labeled human granulocyte colony-stimulating factor (rh-metG-CSF) has been studied by 2D and 3D NMR using...
[NMR paper] Enhanced protein fold recognition using secondary structure information from NMR.
Enhanced protein fold recognition using secondary structure information from NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Enhanced protein fold recognition using secondary structure information from NMR.
Protein Sci. 1999 May;8(5):1127-33
Authors: Ayers DJ, Gooley PR, Widmer-Cooper A, Torda AE
NMR offers...