The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Side Chain Contributions to the Stability of Alpha-Helical Structure in Peptides
Abstract
Short peptides that contain significant α-helical structure in aqueous solution allow the investigation of the role of amino acid side chains in stabilizing or destabilizing α-helix structure. A host-guest system of soluble synthetic peptides was designed that consisted of chains with the block sequence TyrSerGlu 4 Lys 4 X 3 Glu 4 Lys 4 , denoted EXK, in which X represents any "guest" amino acid residue. Circular dichroism spectroscopy indicates that the extent of helicity of these peptides follows the order Ala > Leu > Met > Gln > Ile > Val > Ser > Thr > Asn > Gly. This order differs from both host-guest copolymer values (Met > Ile > Leu > Ala > Gln > Val > Thr > Asn > Ser > Gly) and the tendencies of these amino acids to occur in helices in globular proteins (Ala > Met > Leu > Gln > Ile > Val > Asn, Thr > Ser > Gly), but matches the order found in a series of synthetic coiled-coil α helices, except for Ser. Proton nuclear magnetic resonance analysis of several EXK peptides indicates that these peptides are partially helical, with the helical residues favoring the amino terminus.
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Cites
Prediction of protein conformation
Chou, P. Y., & Fasman, G. D. (1974) · Biochemistry · doi:10.1021/bi00699a002 · Cited by 3,309
Chou, P. Y., & Fasman, G. D. (1974) · Biochemistry · doi:10.1021/bi00699a001 · Cited by 2,172
Cited by
Principles of protein folding — A perspective from simple exact models
Dill, K. A., Bromberg, S., Yue, K., Chan, H. S., Fiebig, K. M., Yee, D. P., & Thomas, P. D. (1995) · Protein Science · doi:10.1002/pro.5560040401 · Cited by 1,525
A Switch Between Two-, Three-, and Four-stranded Coiled Coils in GCN4 Leucine Zipper Mutants
Harbury, P. B., Zhang, T., Kim, P. S., & Alber, T. (1993) · Science · doi:10.1126/science.8248779 · Cited by 1,490
Fersht, A. R., Matouschek, A., & Serrano, L. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90561-w · Cited by 932
Seebach, D., Overhand, M., Kühnle, F. N. M., Martinoni, B., Oberer, L., Hommel, U., & Widmer, H. (1996) · Helvetica Chimica Acta · doi:10.1002/hlca.19960790402 · Cited by 734
Protein Design by Binary Patterning of Polar and Nonpolar Amino Acids
Kamtekar, S., Schiffer, J. M., Xiong, H., Babik, J. M., & Hecht, M. H. (1993) · Science · doi:10.1126/science.8259512 · Cited by 730
Metadata
- Authors
- Lyu, P. C., Liff, M. I., Marky, L. A., & Kallenbach, N. R.
- Venue
- Science
- Published
- 1990-11-02
- Volume
- 250
- Issue
- 4981
- Pages
- 669-673
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1995938191
- Cited by
- 463
- References
- 2
- FWCI
- 13.10
- Type
- journal article
- Language
- en
- Open access
- closed
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- Lyu, P. C., Liff, M. I., Marky, L. A., & Kallenbach, N. R. (1990). Side Chain Contributions to the Stability of Alpha-Helical Structure in Peptides. Science. https://doi.org/10.1126/science.2237416
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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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