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The Use of Proton Chemical Shifts to Define the Solution Structure of a Dimeric Peptide
β Scribed by Bernard Busetta; Philippe Picard
- Publisher
- John Wiley and Sons
- Year
- 1996
- Tongue
- English
- Weight
- 559 KB
- Volume
- 2
- Category
- Article
- ISSN
- 1075-2617
- DOI
- 10.1002/psc.67
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β¦ Synopsis
For flexible peptides, nuclear Overhauser Effects (NOE) experiments do not provide enough information to ensure a correct definition of their solution structure. The use of distance constraints, derived from the knowledge of proton chemical shifts, is developed to restrict the number of possible conformations. In the case of flexible molecules, randomization appears as an important factor of the correct estimation of the chemical shifts from the 3D structure. The refinement of the solution structure of the highly flexible AVP-like parallel dimer is described to illustrate this process.
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The 13C chemical shifts for all of the protonated carbons of the 20 common amino acid residues in the protected linear pentapeptide Gly-Gly-X-Gly-Gly have been obtained in water at low pH as well as in aqueous solution containing 10, 20 and 30% acetonitrile or trifluoroethanol. Dioxane was used as a