Complementary analysis of peptide aggregation by NMR and time-resolved laser spectroscopy

Article Abstract:

The aggregation behavior of naphthyl-substituted beta(12-28) peptide analogues has been investigated using nuclear magnetic resonance and time-resolved laser spectroscopy. To this end, several beta(12-28) derivatives were synthesized in which the phenylalanine residues 19 and/or 20 were replaced with the nonnative amino acid, naphthylalanine to generate different peptides. The use of nuclear magnetic resonance and time-resolved laser spectroscopy was found to be effective for the complementary analysis of peptide aggregation due to their sensitivity to different ranges of molecular motion.

Research, Laser spectroscopy

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Membrane curvature change induced by an antimicrobial peptide detected by (super 31)P exchange NMR

Article Abstract:

The influence of an antimicrobial peptide, protegrin-1 (PG-1) on the curvature and lateral diffusion coefficient (D(sub L)) of phosphocholine bilayers was investigated using one- (1-D) and two-dimensional (2-D) (super 31)P exchange NMR. The simulations of the 2D exchange spectra yielded quantitative reorientation-angle distributions were consistent with the bimodal distributions of the vesicles curvature and the effects of the peptide on the two types of lipid bilayers.

Chemical properties

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Structure, topology, and dynamics of membrane peptides and proteins from solid-state NMR spectroscopy

Article Abstract:

Solid-state NMR spectroscopy is a powerful atomic-resolution probe that is used for determining the structure and dynamics of the membrane proteins. The combination of the solid-state NMR spectroscopy and the resonance assignment methods are important for elucidating the membrane-bound three-dimensional structure and dynamics and the lipid interaction of membrane proteins.

Membrane proteins, Structure

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