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Conformational analysis of apolipoprotein A-I and E-3 based on primary sequence and circular dichroism
Open accessAbstract
The primary and secondary structure of human plasma apolipoprotein A-I and apolipoprotein E-3 have been analyzed to further our understanding of the secondary and tertiary conformation of these proteins and the structure and function of plasma lipoprotein particles. The methods used to analyze the primary sequence of these proteins used computer programs: (a) to identify repeated patterns within these proteins on the basis of conservative substitutions and similarities within the physicochemical properties of each residue; (b) for local averaging, hydrophobic moment, and Fourier analysis of the physicochemical properties; and (c) for secondary structure prediction of each protein carried out using homology, statistical, and information theory based methods. Circular dichroism was used to study purified lipid-protein complexes of each protein and quantitate the secondary structure in a lipid environment. The data from these analyses were integrated into a single secondary structure prediction to derive a model of each protein. The sequence homology within apolipoproteins A-I, E-3, and A-IV is used to derive a consensus sequence for two 11 amino acid repeating sequences in this family of proteins.
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Cites
Comparison of the predicted and observed secondary structure of T4 phage lysozyme
Matthews, B. W. (1975) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(75)90109-9 · Cited by 5,399
Human apolipoprotein E. The complete amino acid sequence
Rall, S. C., Weisgraber, K. H., & Mahley, R. W. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34702-1 · Cited by 741
Three-Dimensional Structure of the LDL Receptor-Binding Domain of Human Apolipoprotein E
Wilson, C., Wardell, M. R., Weisgraber, K. H., Mahley, R. W., & Agard, D. A. (1991) · Science · doi:10.1126/science.2063194 · Cited by 678
Cited by
Stabilization of α-Synuclein Secondary Structure upon Binding to Synthetic Membranes
Davidson, W. S., Jonas, A., Clayton, D. F., & George, J. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9443 · Cited by 1,585
Directed Self-Assembly of Monodisperse Phospholipid Bilayer Nanodiscs with Controlled Size
Denisov, I. G., Grinkova, Y. V., Lazarides, A. A., & Sligar, S. G. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0393574 · Cited by 1,064
The Structure of Amyloid Fibrils by Electron Microscopy and X-Ray Diffraction
SUNDE, M., & BLAKE, C. (1997) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60320-4 · Cited by 767
Structure of apolipoprotein B-100 in low density lipoproteins
Segrest, J. P., Jones, M. K., De Loof, H., & Dashti, N. (2001) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)30267-4 · Cited by 522
Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation
Borhani, D. W., Rogers, D. P., Engler, J. A., & Brouillette, C. G. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12291 · Cited by 434
Metadata
- Authors
- Nolte, R. T., & Atkinson, D.
- Venue
- Biophysical Journal
- Publisher
- Elsevier BV
- Published
- 1992-11
- Volume
- 63
- Issue
- 5
- Pages
- 1221-1239
- ISSN
- 0006-3495 (ISSN-L)
- OpenAlex
- W1969668277
- Cited by
- 161
- References
- 3
- FWCI
- 1.53
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Nolte, R. T., & Atkinson, D. (1992). Conformational analysis of apolipoprotein A-I and E-3 based on primary sequence and circular dichroism. Biophysical Journal. https://doi.org/10.1016/s0006-3495(92)81698-3
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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