2015
DOI: 10.1016/j.ab.2014.12.011
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Construction of a random circular permutation library using an engineered transposon

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Cited by 8 publications
(9 citation statements)
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“…This commentary presents our recent development on combinatorial approaches for the construction of insertional fusion libraries and circular permutation libraries using engineered Mu transposons. 22,23 Transposons for random insertional fusion of protein domains Insertional protein fusion is an advanced engineering approach to generate novel proteins with integrated functions. Three critical parameters that can determine the success of functional integration between fused proteins are the insertion location within the host protein, 24,25 the inter-domain linker length 26,27 and the inter-domain linker composition.…”
Section: Introductionmentioning
confidence: 99%
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“…This commentary presents our recent development on combinatorial approaches for the construction of insertional fusion libraries and circular permutation libraries using engineered Mu transposons. 22,23 Transposons for random insertional fusion of protein domains Insertional protein fusion is an advanced engineering approach to generate novel proteins with integrated functions. Three critical parameters that can determine the success of functional integration between fused proteins are the insertion location within the host protein, 24,25 the inter-domain linker length 26,27 and the inter-domain linker composition.…”
Section: Introductionmentioning
confidence: 99%
“…Also, the ratio of having correctly oriented to inversely oriented insertions of a guest DNA was about 1:1, though slight variation was also observed from run to run. 22,23 Transposons for random circular permutation of proteins Circular permutation is a protein engineering approach that connects the original N-and C-termini of proteins through a linker and, instead, introduces new termini elsewhere in the sequence. 38 As more than 50% of single domain proteins have their N-and C-termini proximal, 39 circular permutation could be an effective tool to generate diversity in the linear order of amino acid sequences.…”
Section: Introductionmentioning
confidence: 99%
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