Prediction of mutant activity and its application in molecular design of tumor necrosis factor-a
Two models for prediction of the activity and stability of site-directed mutagenesis on tumor necrosis factor-α are established. The models are based on straightforward structural considerations, which do not require the elaboration of site-directed mutagenesis on the protein core and the hydrophobi...
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| Published in | Science China. Life sciences Vol. 40; no. 1; pp. 1 - 9 |
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| Main Author | |
| Format | Journal Article |
| Language | English |
| Published |
Dordrecht
Springer Nature B.V
01.02.1997
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| Subjects | |
| Online Access | Get full text |
| ISSN | 1674-7305 1869-1889 |
| DOI | 10.1007/BF02879101 |
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| Abstract | Two models for prediction of the activity and stability of site-directed mutagenesis on tumor necrosis factor-α are established. The models are based on straightforward structural considerations, which do not require the elaboration of site-directed mutagenesis on the protein core and the hydrophobic surface area by analyzing the properties of the mutated amino acid residues. The reliabilities of the models have been tested by analyzing the mutants of tumor necrosis factor-α (TNF-α) whose two leucine residues (L29, L157) were mutated. Based on these models, a TNF-α mutant with high activity was created by molecular design. |
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| AbstractList | Two models for prediction of the activity and stability of site-directed mutagenesis on tumor necrosis factor-α are established. The models are based on straightforward structural considerations, which do not require the elaboration of site-directed mutagenesis on the protein core and the hydrophobic surface area by analyzing the properties of the mutated amino acid residues. The reliabilities of the models have been tested by analyzing the mutants of tumor necrosis factor-α (TNF-α) whose two leucine residues (L29, L157) were mutated. Based on these models, a TNF-α mutant with high activity was created by molecular design. Two models for prediction of the activity and stability of site-directed mutagenesis on tumor necrosis factor-α are established. The models are based on straightforward structural considerations, which do not require the elaboration of sitedirected mutagenesis on the protein core and the hydrophobic surface area by analyzing the pmperties of the mutated amino acid residues. The reliabilities of the models have been tested by analyzing the mutants of tumor necrosis factor-α (TNF-α) whose two leucine residues (L29, L157) were mutated. Based on these models, a TNFα mutant with high activity was created by molecular design.[PUBLICATION ABSTRACT] |
| Author | 唐卫东 奚涛 王波 郭冬林 徐贤秀 朱德煦 |
| AuthorAffiliation | Department of Biochemistry and State Key Laboratory of Pharmaceutical Biotechnology Nanjing University Nanjing 210093 China China |
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| Copyright | Science in China Press 1997 |
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| DOI | 10.1007/BF02879101 |
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| Notes | TANG Weidong XI Tao WANG BoGUO Donglin XU Xianxiuand ZHU Dexu(Department of Biochemistry and State Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, Nanjing 210093, China) 11-5841/Q SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 14 |
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| Snippet | Two models for prediction of the activity and stability of site-directed mutagenesis on tumor necrosis factor-α are established. The models are based on... |
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| SubjectTerms | design factor-α molecular Mutagenesis necrosis prediction Proteins tumor |
| Title | Prediction of mutant activity and its application in molecular design of tumor necrosis factor-a |
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