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Large Variations in 13 C α Chemical Shift Anisotropy in Proteins Correlate with Secondary Structure

✍ Scribed by Tjandra, Nico; Bax, Ad

Book ID
125888109
Publisher
American Chemical Society
Year
1997
Tongue
English
Weight
123 KB
Volume
119
Category
Article
ISSN
0002-7863

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13Cα-NMR assignments of melittin in meth
13Cα-NMR assignments of melittin in methanol and chemical shift correlations with secondary structure
✍ Paul Buckley; Arthur S. Edison; Marvin D. Kemple; Franklyn G. Prendergast 📂 Article 📅 1993 🏛 Springer Netherlands 🌐 English ⚖ 868 KB

Melittin is a naturally occurring hexacosa peptide which forms an amphiphilic helix in methanol, a random coil in water, and a tetramer of helices at basic pH or in the presence of a high salt concentration. The monomeric structure in methanol has been well characterized by proton NMR (Pastore et al