Two distinct structures of alpha-conotoxin GI in aqueous solution
| Autor: | Alexey A. Lugovskoy, Andrey G. Ostrovsky, Vadim T. Ivanov, A.G. Sobol, Konstantin V. Gladky, Victor I. Tsetlin, Alexander S. Arseniev, Innokenty V. Maslennikov |
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| Rok vydání: | 1998 |
| Předmět: |
Models
Molecular Aqueous solution Magnetic Resonance Spectroscopy Basis (linear algebra) Chemistry Stereochemistry Protein Conformation Mollusk Venoms Water Nuclear magnetic resonance spectroscopy In Vitro Techniques Crystallography X-Ray Biochemistry Peptides Cyclic Set (abstract data type) Folding (chemistry) Turn (biochemistry) Solutions Crystallography Protein structure Animals Conotoxin Amino Acid Sequence Conotoxins |
| Zdroj: | European journal of biochemistry. 254(2) |
| ISSN: | 0014-2956 |
| Popis: | The detailed analysis of conformational space of alpha-conotoxin GI in aqueous solution has been performed on the basis of two-dimensional NMR spectroscopy data using multiconformational approach. As the result, two topologically distinct interconvertible sets of GI conformations (populations of 78% and 22%) have been found. A common feature of the two sets is the Asn4-Cys7 beta-turn. The Gly8 to Tyrll region has a structure of right-handed helical turn in the major set and two sequential bends in the minor one. N-terminus and C-terminus also have different orientations, anti-parallel in the major conformational set and parallel in the minor one. An average pairwise rmsd for backbone heavy atoms is 0.56 A in the major set, 0.23 A in the minor, and 1.85 A between the structures of the two sets. The X-ray structure of GI [Guddat, L. W., Martin, J. A., Shan, L., Edmundson, A. B. & Gray, W. R. (1996) Biochemistry 35, 11329 - 11335] has the same folding pattern as the major NMR set, the average backbone rmsd between the two structures being 0.77 A. |
| Databáze: | OpenAIRE |
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