Distance between phosphine-sulfide sidechains of a disubstituted peptide by DRAMA 31P NMR
✍ Scribed by Christopher A Klug; Daniel R Studelska; Guohua Chen; Scott R Gilbertson; Jacob Schaefer
- Book ID
- 104357816
- Publisher
- Elsevier Science
- Year
- 1996
- Tongue
- English
- Weight
- 356 KB
- Volume
- 7
- Category
- Article
- ISSN
- 0926-2040
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✦ Synopsis
Dipolar restoration at the magic angle (DRAMA) has been used to measure the 31P-31P internuclear distance between phosphine-sulfide substituted sidechanins on the fourth and eighth residues of a 12-residue helical peptide. The 7.4 A distance is the same for the peptide lyophilized in bulk or isolated in a cryo- and lyoprotected matrix of poly(ethylene glycol) and sucrose. However, the 31P linewidth for the undiluted peptide is an order of magnitude greater than for the matrix-isolated peptide indicating charge and hydration heterogeneity in the bulk state.