A bioinformatics analysis of disorder content of proteins from the DisProt database has been performed with respect to position of dis- ordered residues. Each protein chain was divided into three parts： N- and C- ter...A bioinformatics analysis of disorder content of proteins from the DisProt database has been performed with respect to position of dis- ordered residues. Each protein chain was divided into three parts： N- and C- terminal parts with each containing 30 amino acid （AA） residues and the middle region containing the remaining AA residues. The results show that in terminal parts, the percentage of disor- dered AA residues is higher than that of all AA residues （17% of disordered AA residues and 11% of all）. We analyzed the percentage of disorder for each of 20 AA residues in the three parts of proteins with respect to their hydropathy and molecular weight. For each AA, the percentage of disorder in the middle part is lower than that in terminal parts which is comparable at the two termini. A new scale of AAs has been introduced according to their disorder content in the middle part of proteins： CIFWMLYHRNVTAGQDSKEP. All big hydrophobic AAs are less frequently disordered, while almost all small hydrophilic AAs are more frequently disordered. The results obtained may be useful for construction and improving predictors for protein disorder.展开更多
基金supported by the Ministry of Education and Science,Republic of Serbia(Project No. 174021)
文摘A bioinformatics analysis of disorder content of proteins from the DisProt database has been performed with respect to position of dis- ordered residues. Each protein chain was divided into three parts： N- and C- terminal parts with each containing 30 amino acid （AA） residues and the middle region containing the remaining AA residues. The results show that in terminal parts, the percentage of disor- dered AA residues is higher than that of all AA residues （17% of disordered AA residues and 11% of all）. We analyzed the percentage of disorder for each of 20 AA residues in the three parts of proteins with respect to their hydropathy and molecular weight. For each AA, the percentage of disorder in the middle part is lower than that in terminal parts which is comparable at the two termini. A new scale of AAs has been introduced according to their disorder content in the middle part of proteins： CIFWMLYHRNVTAGQDSKEP. All big hydrophobic AAs are less frequently disordered, while almost all small hydrophilic AAs are more frequently disordered. The results obtained may be useful for construction and improving predictors for protein disorder.
