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Amphiphilic Secondary Structure: Design of Peptide Hormones
Abstract
Peptide synthesis can be used for elucidating the roles of secondary structures in the specificity of hormones, antigens, and toxins. Intermediate sized peptides with these activities assume amphiphilic secondary structures in the presence of membranes. When models are designed to optimize the amphiphilicity of the secondary structure, stronger interactions can be observed with the synthetic peptides than with the naturally occurring analogs.
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Citations
Cited by
Plasma lipoproteins: apolipoprotein structure and function.
Mahley, R. W., Innerarity, T. L., Rall, S. C., & Weisgraber, K. H. (1984) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)34443-6 · Cited by 1,155
The detection and classification of membrane-spanning proteins
Klein, P., Kanehisa, M., & DeLisi, C. (1985) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(85)90375-x · Cited by 835
Transcending the impenetrable: How proteins come to terms with membranes
von Heijne, G. (1988) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(88)90013-5 · Cited by 466
Primary structure of gonadotropin-releasing hormone from lamprey brain.
Sherwood, N. M., Sower, S. A., Marshak, D. R., Fraser, B. A., & Brownstein, M. J. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)89177-9 · Cited by 253
Peptides from the calcitonin genes: molecular genetics, structure and function
Breimer, L. H., MacIntyre, I., & Zaidi, M. (1988) · Biochemical Journal · doi:10.1042/bj2550377 · Cited by 189
Metadata
- Authors
- Kaiser, E. T., & Kézdy, F. J.
- Venue
- Science
- Published
- 1984-01-20
- Volume
- 223
- Issue
- 4633
- Pages
- 249-255
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2056502094
- Cited by
- 536
- References
- 0
- FWCI
- 16.64
- Type
- journal article
- Language
- en
- Open access
- closed
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- Kaiser, E. T., & Kézdy, F. J. (1984). Amphiphilic Secondary Structure: Design of Peptide Hormones. Science. https://doi.org/10.1126/science.6322295
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
