Determination of the conformational order of lipid membranes from Raman spectroscopy
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Monomolecular layers of lipid extracts of microsomal, mitochondrial outer and inner membranes, and pure lipid species have been used to measure their interaction with apo- and holocytochrome c. Large differences were observed both with respect to the natur ...
American Society for Biochemistry and Molecular Biology1989
Rather than being distributed homogeneously on the cell surface, proteins are probably aggregated in clusters or in specific domains. Some of these domains (lipid rafts) have lipid compositions, which differ from their surrounding membrane. They have been ...
Conformational changes occurring upon membrane binding and subsequent insertion of staphylococcal alpha-toxin were studied using complementary spectroscopic techniques. Experimental conditions were established where binding could be uncoupled from membrane ...
Membrane proteins fulfill many central functions in the biological membrane. The insertion process of these proteins and their structure, which are intimately linked to their function, are not yet well understood. As a model we studied three proteins recon ...
For the first time, the std. free energy change, DG Deg, of a membrane-inserting protein with a leader sequence has been detd. exptl., using M13 procoat protein as an example. The partition coeff. for the distribution of the procoat protein between the aq. ...
A review, with .apprx.75 refs., on (1) structural models of membrane proteins derived from Raman spectroscopy and prediction methods, (2) dynamics of model peptides, (3) proline in transmembrane helixes, and other topics. [on SciFinder (R)] ...
Aerolysin secreted by the human pathogen Aeromonas hydrophila belongs to a group of bacterial toxins that are hemolytic and form channels in biological membranes. The toxin is secreted as an inactive precursor proaerolysin that must be proteolytically proc ...
Time-resolved fluorescence anisotropy (FA) measurements are reported for 5 helical, bilayer-spanning heneicosapeptides, each contg. 1 tryptophan (Trp) at sequence positions 1, 6, 11, 16, and 21, resp. The FA decay reflected 2 mol. processes in all cases, l ...
Time-resolved fluorescence anisotropy of the single tryptophan (Trp) residue of melittin was measured to assess the orientational fluctuations of the protein in lipid membranes above and below the lipid phase transition temp. (Tt). In phospholipid vesicles ...