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  • 1
    Electronic Resource
    Electronic Resource
    Detergent removal by non-polar polystyrene beads (1998)
    Springer
    European biophysics journal 27 (1998), S. 305-319 
    Details
    ISSN: 1432-1017
    Keywords: Key words Bio-Beads ; Detergents ; Liposomes ; Proteoliposomes ; Reconstitution ; 2 D crystallization ; Membrane proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract Detergent removal from lipid-protein-detergent micellar solutions is the most successful strategy for reconstitution of integral membrane proteins into proteoliposomes or into two-dimensional crystals. This review establishes the potential of polystyrene beads as a simple alternative to other conventional detergent removing strategies such as dialysis, gel chromatography and dilution. Kinetics and equilibrium aspects of removal of different detergents by hydrophobic adsorption onto polystyrene beads have been systematically investigated. A mechanism of adsorption onto polystyrene beads is proposed and provide useful information about the use of these beads in reconstitution experiments. The usefulness of this detergent removal strategy to produce quasi-ideal proteoliposomes is evaluated by considering the morphology and the size of the reconstituted vesicles, the homogeneity in size and protein distribution, the final protein orientation and the permeability of resulting proteoliposomes. Finally, the advantages of detergent removal by polystyrene beads as an alternative to conventional dialysis in two-dimensional crystallization trials are evaluated through review of recent structural reconstitution studies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002490050138
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  • 2
    Electronic Resource
    Electronic Resource
    A high-resolution 1H NMR approach for structure determination of membrane peptides and proteins in non-deuterated detergent: Application to mastoparan X solubilized in n-octylglucoside (1995)
    Springer
    Journal of biomolecular NMR 5 (1995), S. 345-352 
    Details
    ISSN: 1573-5001
    Keywords: Selective excitation ; 2D NMR ; Membrane proteins ; Detergents
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Application of 1H 2D NMR methods to solubilized membrane proteins and peptides has up to now required the use of selectively deuterated detergents. The unavailability of any of the common biochemical detergents in deuterated form has therefore limited to some extent the scope of this approach. Here a 1H NMR method is described which allows structure determination of membrane peptides and small membrane proteins by 1H 2D NMR in any type of non-deuterated detergent. The approach is based on regioselective excitation of protein resonances with DANTE-Z or spin-pinging pulse trains. It is shown that regioselective excitation of the amide-aromatic region of solubilized membrane proteins and peptides leads to an almost complete suppression of the two orders of magnitude higher contribution of the protonated detergent to the 1H NMR spectrum. Consistently TOCSY, COSY and NOESY sequences incorporating such regioselective excitation in the F2 dimension yield protein 1H 2D NMR spectra of quality comparable to those obtained in deuterated detergents. Regioselective TOCSY and NOESY spectra display all through-bond and through-space correlations within amide-aromatic protons and between these protons and aliphatic and α-protons. Regioselective COSY spectra provide scalar coupling constants between amide and α-protons. Application of the method to the membrane-active peptide mastoparan X, solubilized in n-octylglucoside, yields complete sequence-specific assignments and extensive secondary structure-related spatial proximities and coupling constants. It is shown that mastoparan adopts an α-helical conformation when bound to nonionic detergent micelles. The present method is expected to increase the applicability of 1H solution NMR methods to membrane proteins and peptides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00182276
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    Paper (German National Licenses)
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