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The Folding Type of a Protein Is Relevant to the Amino Acid Composition
Open accessAbstract
The folding types of 135 proteins, the three-dimensional structures of which are known, were analyzed in terms of the amino acid composition. The amino acid composition of a protein was expressed as a point in a multidimensional space spanned with 20 axes, on which the corresponding contents of 20 amino acids in the protein were represented. The distribution pattern of proteins in this composition space was examined in relation to five folding types, alpha, beta, alpha/beta, alpha + beta, and irregular type. The results show that amino acid compositions of the alpha, beta, and alpha/beta types are located in different regions in the composition space, thus allowing distinct separation of proteins depending on the folding types. The points representing proteins of the alpha + beta and irregular types, however, are widely scattered in the space, and the existing regions overlap with those of the other folding types. A simple method of utilizing the "distance" in the space was found to be convenient for classification of proteins into the five folding types. The assignment of the folding type with this method gave an accuracy of 70% in the coincidence with the experimental data.
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Cited by
Amino Acid Preferences for Specific Locations at the Ends of α Helices
Richardson, J. S., & Richardson, D. C. (1988) · Science · doi:10.1126/science.3381086 · Cited by 1,364
Some remarks on protein attribute prediction and pseudo amino acid composition
Chou, K.-C. (2011) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2010.12.024 · Cited by 1,225
Recent progress in protein subcellular location prediction
Chou, K.-C., & Shen, H.-B. (2007) · Analytical Biochemistry · doi:10.1016/j.ab.2007.07.006 · Cited by 770
Chou, K.-C., & Cai, Y.-D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204161200 · Cited by 483
A novel approach to predicting protein structural classes in a (20–1)‐D amino acid composition space
Chou, K. (1995) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340210406 · Cited by 428
Metadata
- Authors
- NAKASHIMA, H., NISHIKAWA, K., & OOI, T.
- Venue
- The Journal of Biochemistry
- Publisher
- Oxford University Press (OUP)
- Published
- 1986-01
- Volume
- 99
- Issue
- 1
- Pages
- 153-162
- ISSN
- 0021-924X (ISSN-L)
- 1756-2651
- OpenAlex
- W1821507858
- Cited by
- 458
- References
- 0
- FWCI
- 2.35
- Type
- journal article
- Language
- en
- Open access
- green
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- NAKASHIMA, H., NISHIKAWA, K., & OOI, T. (1986). The Folding Type of a Protein Is Relevant to the Amino Acid Composition. The Journal of Biochemistry. https://doi.org/10.1093/oxfordjournals.jbchem.a135454
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