gt4sd.properties.proteins.functions module¶
Summary¶
Functions:
Computes the aliphatic index of a protein. |
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Computes aromaticity of the protein (relative frequency of Phe+Trp+Tyr). |
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Computes the Boman index of a protein (sum of solubility values of all residues). |
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Computes the charge of a protein. |
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Computes the charge density of a protein. |
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Computes the hydrophobicity of a protein, relative freq. |
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Calculates the protein instability. |
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Computes the isoelectric point of every residue and aggregates. |
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Retrieves the number of residues of a protein. |
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Computes the molecular weight of a protein. |
Reference¶
- molecular_weight(protein, amide=False)[source]¶
Computes the molecular weight of a protein.
- Return type
float
- boman_index(protein)[source]¶
Computes the Boman index of a protein (sum of solubility values of all residues).
Boman, H. G. (2003). Antibacterial peptides: basic facts and emerging concepts. Journal of internal medicine, 254(3), 197-215.
- Return type
float
- aliphatic_index(protein)[source]¶
Computes the aliphatic index of a protein. Measure of thermal stability.
Ikai, A. (1980). Thermostability and aliphatic index of globular proteins. The Journal of Biochemistry, 88(6), 1895-1898.
- Return type
float
- hydrophobic_ratio(protein)[source]¶
Computes the hydrophobicity of a protein, relative freq. of A,C,F,I,L,M & V.
- Return type
float
- charge(protein, ph=7.0, amide=False)[source]¶
Computes the charge of a protein.
Bjellqvist, B., Hughes, G. J., Pasquali, C., Paquet, N., Ravier, F., Sanchez, J. C., … & Hochstrasser, D. (1993). The focusing positions of polypeptides in immobilized pH gradients can be predicted from their amino acid sequences. Electrophoresis, 14(1), 1023-1031.
- Return type
float
- charge_density(protein, ph=7.0, amide=False)[source]¶
Computes the charge density of a protein.
Bjellqvist, B., Hughes, G. J., Pasquali, C., Paquet, N., Ravier, F., Sanchez, J. C., … & Hochstrasser, D. (1993). The focusing positions of polypeptides in immobilized pH gradients can be predicted from their amino acid sequences. Electrophoresis, 14(1), 1023-1031.
- Return type
float
- isoelectric_point(protein, amide=False)[source]¶
Computes the isoelectric point of every residue and aggregates.
- Return type
float
- aromaticity(protein)[source]¶
Computes aromaticity of the protein (relative frequency of Phe+Trp+Tyr).
Lobry, J. R., & Gautier, C. (1994). Hydrophobicity, expressivity and aromaticity are the major trends of amino-acid usage
in 999 Escherichia coli chromosome-encoded genes.
Nucleic acids research, 22(15), 3174-3180.
- Return type
float
- instability(protein)[source]¶
Calculates the protein instability.
Guruprasad, K., Reddy, B. B., & Pandit, M. W. (1990). Correlation between stability of a protein and its dipeptide composition: a novel
approach for predicting in vivo stability of a protein from its primary sequence.
Protein Engineering, Design and Selection, 4(2), 155-161.
- Return type
float