Influence of Dynamics on The Analysis of Solid-State NMR Data From Membrane-bound Peptides
✍ Scribed by Strandberg, Erik; Esteban-Martin, Santi; Salgado, Jesús; Ulrich, Anne S.
- Book ID
- 122166479
- Publisher
- Biophysical Society
- Year
- 2009
- Tongue
- English
- Weight
- 97 KB
- Volume
- 96
- Category
- Article
- ISSN
- 0006-3495
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## Abstract Many membrane peptides and protein domains contain functionally important cationic Arg and Lys residues, whose insertion into the hydrophobic interior of the lipid bilayer encounters significant energy barriers. To understand how these cationic molecules overcome the free energy barrier
under 4.5 kHz MAS. Two-dimensional LG-CP and DIPSHIFT experiments were used to measure CÀH dipolar couplings and the ROCSA experiment was used to measure the 13 C NMR CSA values. Further details of orientation simulations are given in the Supporting Information.