REFERENCES

  1. Buchko, G.W., A. Rozek, Q. Zhong and R.J. Cushley (1995). Sequence Specific 1H NMR Assignments and Secondary Structure of a Lipid Associating Peptide from ApoC-I in Dodecylphosphocholine Micelles. An NMR Study of the Amphipathic Helix Motif. Peptide Res., 8:86-94.

  2. Rozek, A., G.W. Buchko and R. J. Cushley (1995). Conformation of Two Peptides Corresponding to Human Apolipoprotein C-I Residues 7-24 and 35-53 in the Presence of Sodium Dodecylsulfate by CD and NMR Spectroscopy. Biochemistry, 34:7401-7408.

  3. Buchko, G.W., A. Rozek, P. Kanda and R.J. Cushley (1995). A Structural Comparison of Two Peptides Corresponding to Human and Baboon Apolipoprotein C-I Residues 1-38. J. Cell. Biochem., 21B:42.

  4. Pierens, G.K., G.W. Buchko, G. Wang, W.D. Treleaven, A Rozek and R.J. Cushley (1995). NMR Structural Studies of Amphipathic Helices. Bull. Magn. Reson., 17:292-293.

  5. Buchko, G.W., W.D. Treleaven, S.J. Dunne, A.S. Tracey and R.J. Cushley (1996). Structural Studies of a Peptide Activator of Human Lecithin:cholesterol Acyl Transferase. J. Biol. Chem., 271:3039-3045.

  6. Buchko, G.W., G. Wang, G.K. Pierens and R.J. Cushley (1996). Conformational Studies of a de novo Amphipathic Peptide Corresponding to Human Apolipoprotein A-II Residues 18-30 with a C-terminal Lipid-binding Motif EWLNS. Internat. J. Pept. Res., 48:21-30.

  7. Wang, G., W.D. Treleaven and R.J. Cushley (1996). Conformation of Human Serum Apolipoprotein A-I(166-185) in the Presence of Sodium Dodecyl Sulfate by 1H-NMR and CD. Evidence for Specific Peptide-Lipid Interactions. Biochim. Biophys. Acta, 1301:174-184.

  8. Wang, G., G.K. Pierens, W.D. Treleaven, J.T. Sparrow and R.J. Cushley (1996). Conformations of Human Apolipoprotein E(263-286) and E(267-289) in Aqueous Solutions of Sodium Dodecyl Sulfate by CD and 1H NMR. Biochemistry, 35:10358-10366.

  9. Rozek, A., G.W. Buchko, P. Kanda and R.J. Cushley (1997). Conformational Studies of the N-Terminal Lipid-associating Domain of Human Apolipoprotein C-I by CD and 1H NMR. Protein Science, 6:1858-1868.

  10. Buchko, G.W., A. Rozek, G. Wang, J.J. Frohlich and R.J. Cushley (1997). High Resolution 1H NMR Spectra of Human Apolipoprotein C-III2 using DPC to Model the Lipoprotein Environment. Prot. Pept. Lett., 4:47-54.

  11. Wang, G., J.T. Sparrow and R.J. Cushley (1997). The Helix-hinge-helix Structural Motif in Human Apolipoprotein A-I Determined by NMR Spectroscopy. Biochemistry, 36:13657-13666.

  12. Shaw, R.A., G.W. Buchko, G. Wang, A. Rozek, W.D. Treleaven, H.H. Mantsch, H.H. and R.J. Cushley (1997). Infrared Spectroscopy of Human Apolipoprotein Fragments in SDS/D2O: Relative Lipid-Binding Affinities and a Novel Amide I Assignment. Biochemistry, 36:14531-14538.

  13. Buchko, G.W., A. Rozek, D.W. Hoyt, R.J. Cushley and M.A. Kennedy (1998). The Use of Sodium Dodecyl Sulfate to Model the Lipoprotein Environment. Evidence for Peptide-SDS Complexes Using Pulsed-Field-Gradient NMR Spectroscopy. Biochim. Biophys. Acta, 1392:101-108.

  14. Rozek, A., J.T. Sparrow, K.H. Weisgraber and R.J. Cushley (1998). Sequence Specific 1H NMR Resonance Assignments and Secondary Structure of Human Apolipoprotein C-I in the Presence of Sodium Dodecyl Sulfate, Biochem. Cell Biol. NMR Special Issue,  76: 267-275.

  15. Rozek, A., J.T. Sparrow, K.H. Weisgraber and R.J. Cushley (1999). The Structure of Human Apolipoprotein C-I Determined by NMR in a Lipid-mimetic Environment.  Biochemistry, 38: 14475-14484.  Download at: http://pubs.acs.org/reprint-request?bi982966h/h2jb
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Bob
Dr. Robert J. Cushley
Biological NMR Group
Simon Fraser University
Institute of Molecular Biology and Biochemistry
Burnaby, British Columbia, Canada V5A 1S6
cushley@sfu.ca
Institute of Molecular Biology and Biochemistry, Simon Fraser University

Created by Kathy Cushley
last modified: June 1, 1998

URL: http://www.sfu.ca/cushley