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Engineering new functions and altering existing functions
Structural and mechanistic information, sequence comparisons, and site-directed mutagenesis data continue to provide a basis for the rational design of new protein functions and the alteration of existing functions. Random mutagenesis and ‘directed evolution’ approaches, however, are making signific...
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Published in: | Current opinion in structural biology 1996-08, Vol.6 (4), p.513-518 |
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container_end_page | 518 |
container_issue | 4 |
container_start_page | 513 |
container_title | Current opinion in structural biology |
container_volume | 6 |
creator | Shao, Zhixin Arnold, Frances H |
description | Structural and mechanistic information, sequence comparisons, and site-directed mutagenesis data continue to provide a basis for the rational design of new protein functions and the alteration of existing functions. Random mutagenesis and ‘directed evolution’ approaches, however, are making significant headway in solving protein engineering problems, proving highly practical for tuning properties such as enzyme substrate specificity. |
doi_str_mv | 10.1016/S0959-440X(96)80117-5 |
format | article |
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ispartof | Current opinion in structural biology, 1996-08, Vol.6 (4), p.513-518 |
issn | 0959-440X 1879-033X |
language | eng |
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source | ScienceDirect Journals |
subjects | Binding Sites Directed Molecular Evolution Green Fluorescent Proteins Luminescent Proteins - chemistry Protein Engineering Proteins - chemistry Proteins - metabolism Structure-Activity Relationship Substrate Specificity |
title | Engineering new functions and altering existing functions |
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