The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Internal packing of helical membrane proteins
Open accessAbstract
Helix packing is important in the folding, stability, and association of membrane proteins. Packing analysis of the helical portions of 7 integral membrane proteins and 37 soluble proteins show that the helices in membrane proteins have higher packing values (0.431) than in soluble proteins (0.405). The highest packing values in integral membrane proteins originate from small hydrophobic (G and A) and small hydroxyl-containing (S and T) amino acids, whereas in soluble proteins large hydrophobic and aromatic residues have the highest packing values. The highest packing values for membrane proteins are found in the transmembrane helix–helix interfaces. Glycine and alanine have the highest occurrence among the buried amino acids in membrane proteins, whereas leucine and alanine are the most common buried residue in soluble proteins. These observations are consistent with a shorter axial separation between helices in membrane proteins. The tight helix packing revealed in this analysis contributes to membrane protein stability and likely compensates for the lack of the hydrophobic effect as a driving force for helix–helix association in membranes.
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Cites
Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc 1 Complex
Iwata, S., Lee, J. W., Okada, K., Lee, J. K., Iwata, M., Rasmussen, B., Link, T. A., Ramaswamy, S., & Jap, B. K. (1998) · Science · doi:10.1126/science.281.5373.64 · Cited by 1,253
Cited by
Hanson, M. A., Cherezov, V., Griffith, M. T., Roth, C. B., Jaakola, V.-P., Chien, E. Y. T., Velasquez, J., Kuhn, P., & Stevens, R. C. (2008) · Structure · doi:10.1016/j.str.2008.05.001 · Cited by 933
Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs
Senes, A., Engel, D. E., & DeGrado, W. F. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2004.07.007 · Cited by 434
Multipass membrane protein structure prediction using Rosetta
Yarov‐Yarovoy, V., Schonbrun, J., & Baker, D. (2006) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.20817 · Cited by 323
Gieswein, C. E., Sharom, F. J., & Wildeman, A. G. (2003) · Virology · doi:10.1016/s0042-6822(03)00296-4 · Cited by 27
Metadata
- Authors
- Eilers, M., Shekar, S. C., Shieh, T., Smith, S. O., & Fleming, P. J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2000-05-23
- Volume
- 97
- Issue
- 11
- Pages
- 5796-5801
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2063044149
- Cited by
- 257
- References
- 1
- FWCI
- 6.20
- Type
- journal article
- Language
- en
- Open access
- green
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- Eilers, M., Shekar, S. C., Shieh, T., Smith, S. O., & Fleming, P. J. (2000). Internal packing of helical membrane proteins. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.97.11.5796
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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.
