Relation of amino acid composition and the moffitt parameters to the secondary structure of proteins
β Scribed by D. E. Goldsack
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1969
- Tongue
- English
- Weight
- 721 KB
- Volume
- 7
- Category
- Article
- ISSN
- 0006-3525
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β¦ Synopsis
A statistical analysis c the relation between the amino acid composition of proteins and the amount of helical secondary structure as characterized by the Moffitt bo parameter has shown a high degree of correlation of the bo parameter with those amino acids whose homopolymers can form helical structures. Using the data for 107 proteins, a linear relation was found between bo and the sum of the residue percentages of alanine, arginine, aspartic acid, cysteine, glutamic acid, leucine, andlysine. A statistical analysis of the Moffitt a. parameter, on the other hand, showed no statistically significant grouping of amino acids in relation to the amount of secondary @ structure in a protein.
A plot of bo versus a. -a:, where a? represents the a0 parameter for a fully denatured protein, for 55 proteins showed distinct nonlinearity. This nonlinearity was postulated to be due to presence of @ structure, and a nomagram was constructed which allowed a semiquantitative estimate of the amount of helical and @-type secondary structures from the 60 Venus a0a? plot.
π SIMILAR VOLUMES
Knowledge of amino acid composition, alone, is verified here to be sufficient for recognizing the structural class, alpha, beta, alpha + beta, or alpha/beta of a given protein with an accuracy of 81%. This is supported by results from exhaustive enumerations of all conformations for all sequences of
## Abstract Correspondence analysis of 28 proteomes selected to span the entire realm of prokaryotes revealed universal biases in the proteins' amino acid distribution. Integral Inner Membrane Proteins always form an individual cluster, which can then be used to predict protein localisation in unkn