Circular dichroism and Raman spectroscopic study of the spider venom toxin V50F17
| Autor: | Maurice Berjot, Guy Lippens, C Dhalluin, Alain J.P. Alix, Manuel Dauchez |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
chemistry.chemical_classification
Circular dichroism Segestria florentina Molecular model biology Globular protein Stereochemistry Organic Chemistry biology.organism_classification Analytical Chemistry Inorganic Chemistry symbols.namesake chemistry Side chain symbols Raman spectroscopy Protein secondary structure Spectroscopy Cysteine |
| Zdroj: | Journal of Molecular Structure. :427-430 |
| ISSN: | 0022-2860 |
| DOI: | 10.1016/s0022-2860(98)00917-x |
| Popis: | V50F17 is a small 45 amino acid neurotoxin fractionated (F17) from the venom V50 of the spider Segestria florentina , which has eight cysteine residues constituting four disulfide bridges. Using circular dichroism data and vibrational Raman data at both pH 2.9 and 7.0 and preliminary NMR results obtained at pH 2.9, we derived structural information for this small protein. From these data, it is seen that it is possible to characterise well the local conformation of the disulfide bridges and the overall shape of the globular protein. Moreover, using optical spectroscopic data, it is shown that consequent local and/or global modifications are obtained on changing the pH. Results of the secondary structure states, the local conformations of the disulfide bridges, the exposure of side chains of residues and particularly of Tyr41 are discussed. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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