The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
A Thermodynamic Scale for the Helix-Forming Tendencies of the Commonly Occurring Amino Acids
Abstract
Amino acids have distinct conformational preferences that influence the stabilities of protein secondary and tertiary structures. The relative thermodynamic stabilities of each of the 20 commonly occurring amino acids in the α-helical versus random coil states have been determined through the design of a peptide that forms a noncovalent α-helical dimer, which is in equilibrium with a randomly coiled monomeric state. The α helices in the dimer contain a single solvent-exposed site that is surrounded by small, neutral amino acid side chains. Each of the commonly occurring amino acids was substituted into this guest site, and the resulting equilibrium constants for the monomer-dimer equilibrium were determined to provide a list of free energy difference (ΔΔ G °) values.
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Citations
Cites
Chou, P. Y., & Fasman, G. D. (1974) · Biochemistry · doi:10.1021/bi00699a001 · Cited by 2,172
Cited by
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
Using collective variables to drive molecular dynamics simulations
Fiorin, G., Klein, M. L., & Hénin, J. (2013) · Molecular Physics · doi:10.1080/00268976.2013.813594 · Cited by 1,053
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
Elucidating the folding problem of helical peptides using empirical parameters
Muñoz, V., & Serrano, L. (1994) · Nature Structural & Molecular Biology · doi:10.1038/nsb0694-399 · Cited by 721
Binz, H. K., Stumpp, M. T., Forrer, P., Amstutz, P., & Plückthun, A. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00896-9 · Cited by 589
Metadata
- Authors
- O'Neil, K. T., & DeGrado, W. F.
- Venue
- Science
- Published
- 1990-11-02
- Volume
- 250
- Issue
- 4981
- Pages
- 646-651
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1968673134
- Cited by
- 1,188
- References
- 1
- FWCI
- 19.04
- Type
- journal article
- Language
- en
- Open access
- closed
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- O'Neil, K. T., & DeGrado, W. F. (1990). A Thermodynamic Scale for the Helix-Forming Tendencies of the Commonly Occurring Amino Acids. Science. https://doi.org/10.1126/science.2237415
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
