Abstract
A novel approach is being developed to probe the secondary structure of membrane proteins and peptides qualitatively utilizing the three-pulse Electron Spin Echo Envelope Modulation (ESEEM) pulse sequence. In order to demonstrate the practicality of this biophysical technique, the M2delta subunit of AChR (α-helical), KAGAKI (β-sheet) and VRL8 (310-helix) peptides were incorporated into phospholipids bicelles to probe their secondary structure with ESSEM spectroscopy. Utilizing site-directed spin-labeling (SDSL) coupled with deuterated amino acid labeling of the peptides, the corresponding ESEEM spectra reveal characteristic patterns for α-helix, β-sheet and 310-helical structures. This ESSEM secondary structural approach can be used with different deuterated amino acids and provide pertinent qualitative structural information on membrane proteins in a short period of time (10 minutes) with small amounts of sample (30 μg).
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