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פותח על ידי קלירמאש פתרונות בע"מ -
Biased random mutagenesis of peptides: Determination of mutation frequency by computer simulation
Year:
1995
Authors :
אופיר, רון
;
.
Volume :
8
Co-Authors:
Ophir, R., Department of Cell Research and Immunology, George S.Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv, Tel Aviv 69978, Israel
Gershoni, J.M., Department of Cell Research and Immunology, George S.Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv, Tel Aviv 69978, Israel
Facilitators :
From page:
143
To page:
146
(
Total pages:
4
)
Abstract:
Cassette mutagenesis is a method of protein engineering which generates a wide diversity of genetic variants that can be subjected to either selection or screening. As long as the target sequence to be modified is kept short (corresponding to four to six amino acids), complete combinatorial libraries can be produced. A major problem arises when longer peptides are to be engineered for desired functions. In such situations the production of a limited collection of variants can be helpful; thus, biased random mutagenesis and 'doping schemes' have been reported previously. Here we describe a computer algorithm that enables the determination of the degree of phosphoramidite contamination of nucleotide precursor reservoirs. Through simulation of biological translation, the algorithm allows the prediction of the effect of contamination levels on the number of mutations to occur for any given peptide sequence. In this study the cholinergic binding site was used as a model sequence (22 amino acids). Considerations, based on the computer program, are discussed regarding the efficient design of phage-display combinatorial libraries. © 1995 Oxford University Press.
Note:
Related Files :
Amides
Animal
Binding Sites
computer program
computer simulation
genetic engineering
peptides
phosphoramidic acid derivative
עוד תגיות
תוכן קשור
More details
DOI :
10.1093/protein/8.2.143
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
32546
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 01:10
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Scientific Publication
Biased random mutagenesis of peptides: Determination of mutation frequency by computer simulation
8
Ophir, R., Department of Cell Research and Immunology, George S.Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv, Tel Aviv 69978, Israel
Gershoni, J.M., Department of Cell Research and Immunology, George S.Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv, Tel Aviv 69978, Israel
Biased random mutagenesis of peptides: Determination of mutation frequency by computer simulation
Cassette mutagenesis is a method of protein engineering which generates a wide diversity of genetic variants that can be subjected to either selection or screening. As long as the target sequence to be modified is kept short (corresponding to four to six amino acids), complete combinatorial libraries can be produced. A major problem arises when longer peptides are to be engineered for desired functions. In such situations the production of a limited collection of variants can be helpful; thus, biased random mutagenesis and 'doping schemes' have been reported previously. Here we describe a computer algorithm that enables the determination of the degree of phosphoramidite contamination of nucleotide precursor reservoirs. Through simulation of biological translation, the algorithm allows the prediction of the effect of contamination levels on the number of mutations to occur for any given peptide sequence. In this study the cholinergic binding site was used as a model sequence (22 amino acids). Considerations, based on the computer program, are discussed regarding the efficient design of phage-display combinatorial libraries. © 1995 Oxford University Press.
Scientific Publication
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