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Deuterium/Hydrogen Exchange Factors Measured by Solution Nuclear Magnetic Resonance Spectroscopy as Indicators of the Structure and Topology of Membrane Proteins

Deuterium/Hydrogen Exchange Factors Measured by Solution Nuclear Magnetic Resonance Spectroscopy as Indicators of the Structure and Topology of Membra

Deuterium/Hydrogen Exchange Factors Measured by Solution Nuclear Magnetic Resonance Spectroscopy as Indicators of the Structure and Topology of Membrane Proteins   (Citations: 15)
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Deuterium/hydrogen exchange factors (χ) were measured for the backbone amide sites of the membrane-bound forms of the 50-residue fd coat protein and the 23-residue magainin2 peptide in lipid micelles by solution nuclear magnetic resonance spectroscopy. By combining kinetic and thermodynamic effects, deuterium/hydrogen exchange factors overcome the principal limitations encountered in the measurements of kinetic protection factors and thermodynamic fractionation factors for membrane proteins. The magnitudes of the exchange factors can be correlated with the structure and topology of membrane-associated polypeptides. In fd coat protein, residues in the transmembrane helix have exchange factors that are substantially smaller than those in the amphipathic surface helix or the loop connecting the two helices. For the amphipathic helical peptide, magainin2, the exchange factors of residues exposed to the solvent are appreciably larger than those that face the hydrocarbon portion of membrane bilayers. These examples demonstrate that deuterium/hydrogen exchange factors can be measured by solution NMR spectroscopy and used to identify residues in transmembrane helices as well as to determine the polarity of amphipathic helices in membrane proteins.
Journal: Biophysical Journal - BIOPHYS J , vol. 82, no. 4, pp. 2176-2183, 2002
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    • ...To determine which residues are in the helical transmembrane region the method of deuterium exchange was used (Veglia et al. 2002)...

    Gabriel A. Cook. NMR studies of p7 protein from hepatitis C virus

    • ...For example, only ;24% of the HIV-1 virus Vpu protein TMD hydrogens exchanged in lipid bilayers (45), the fd coat protein TMD was protected from exchange in detergent micelles (46), only ;24% of a peptide corresponding to the phospholemman TMD exchanged in lipid bilayers (47), the EmrE multidrug transporter amides proved mostly resistant to exchange (48), and only 45% of the full-length SliK potassium channel amides were prone to exchange ...

    Walter Stelzeret al. Sequence-Specific Conformational Flexibility of SNARE Transmembrane He...

    • ...The dynamic properties of each domain in AFA-PLB are also correlated with its thermodynamic stability as assessed by hydrogen/deuterium exchange factors (Veglia et al., 2002)...
    • ...Biophysical Journal 87(2) 1205–1214 where y is the peak volume, C is a normalization factor, and X is the mole fraction of H2O in the solution (Veglia et al., 2002)...
    • ...These slow exchange dynamics are also supported by the proton/deuterium exchange factors (x) (Veglia et al., 2002) measured at different temperatures (Fig. 5). Small values for these exchange factors have been correlated with the most thermodynamically stable (rigid) regions of membrane proteins, whereas higher exchange factors are indicative of...
    • ...residues that are more exposed to solvent exchange, and less thermodynamically stable (mobile) (Veglia et al., 2002)...

    Emily E. Metcalfeet al. 1H/ 15N Heteronuclear NMR Spectroscopy Shows Four Dynamic Domains for ...

    • ...The experiments were performed at 508C and 378C (Veglia et al., 2002)...
    • ...The hydrogen/deuterium (H/D) exchange factor method was used to analyze the hydrogen bonds (Veglia et al., 2002)...
    • ...The residues located in the cytoplasmic region of PLB (4‐18) have a value of xav ; 1.3, which is typical of helices absorbed on the surface of micelles (Veglia et al., 2002), with a gradual decrease in value going from residues 5 through 19...

    Jamillah Zamoonet al. NMR Solution Structure and Topological Orientation of Monomeric Phosph...

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