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
We had previously identified a novel protein termed Rwddl whose expression in thymus is decreased in aged or oxidatively stressed mice. In the present study, we found that Rwddl expressed in both prokaryotic and eukar...We had previously identified a novel protein termed Rwddl whose expression in thymus is decreased in aged or oxidatively stressed mice. In the present study, we found that Rwddl expressed in both prokaryotic and eukaryotic ceils showed a slower migration rate on SDS-PAGE gel. In addition, Rwddl was more sensitive to proteinase proteolysis. Furthermore, being a highly acidic protein which contains an RWD domain, Rwddl shared a high level of sequence similarity with Gir2, a member of the intrinsically unstructured protein （IUP）. These findings suggest that Rwddl is a novel member of the IUP family.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.
基金a grant from theJapan Institute for the Control of Aging (JaICA 2000-2003)a fund from the National Natural Science Foundation of China (No. 30471589) to Dr. Wei He.
文摘We had previously identified a novel protein termed Rwddl whose expression in thymus is decreased in aged or oxidatively stressed mice. In the present study, we found that Rwddl expressed in both prokaryotic and eukaryotic ceils showed a slower migration rate on SDS-PAGE gel. In addition, Rwddl was more sensitive to proteinase proteolysis. Furthermore, being a highly acidic protein which contains an RWD domain, Rwddl shared a high level of sequence similarity with Gir2, a member of the intrinsically unstructured protein （IUP）. These findings suggest that Rwddl is a novel member of the IUP family.
