![]() ![]() ![]() To address this challenge, we developed a computational protocol to significantly reduce the complementarity of DNA sequences encoding TRs called TReSR (for Tandem Repeat DNA Sequence Redesign). However, the repetitive nature of DNA sequences encoding TR motifs complicates their synthesis and mutagenesis by traditional molecular biology workflows commonly employed by protein engineers and synthetic biologists. ![]() These functionalities make protein TR domains an attractive component for the modular design of protein constructs. They are found in approximately 14% of all proteins and are implicated in diverse biological functions facilitating both structured and disordered protein-protein and protein-DNA interactions. Protein tandem repeats (TRs) are motifs comprised of near-identical contiguous sequence duplications. ![]()
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