Difference between revisions of "Part:BBa K4665175"
 
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<partinfo>BBa_K4665175 short</partinfo>
 
 
===GGGGS linker===
 
===GGGGS linker===
  
 
This is a flexible linker made of 4 glycine repeats followed by a serine amino acid, typically used for attaching two protein domains of a fusion protein. The glycine-serine linker incorporates both flexible and hydrophilic elements, preventing the formation of secondary structures and reducing the chance that the linker will interfere with the folding and function of the connected protein domains (van Rosmalen et al., 2017).
 
This is a flexible linker made of 4 glycine repeats followed by a serine amino acid, typically used for attaching two protein domains of a fusion protein. The glycine-serine linker incorporates both flexible and hydrophilic elements, preventing the formation of secondary structures and reducing the chance that the linker will interfere with the folding and function of the connected protein domains (van Rosmalen et al., 2017).
  
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===References===
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===Usage and Biology===
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Van Rosmalen, M. M., Krom, M., & Merkx, M. (2017). Tuning the Flexibility of Glycine-Serine Linkers To Allow Rational Design of Multidomain Proteins. Biochemistry, 56(50), 6565–6574. https://doi.org/10.1021/acs.biochem.7b00902
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<span class='h3bb'>Sequence and Features</span>
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<partinfo>BBa_K4665175 SequenceAndFeatures</partinfo>
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===Functional Parameters===
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<partinfo>BBa_K4665175 parameters</partinfo>
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Latest revision as of 14:15, 8 October 2023

GGGGS linker

This is a flexible linker made of 4 glycine repeats followed by a serine amino acid, typically used for attaching two protein domains of a fusion protein. The glycine-serine linker incorporates both flexible and hydrophilic elements, preventing the formation of secondary structures and reducing the chance that the linker will interfere with the folding and function of the connected protein domains (van Rosmalen et al., 2017).

References

Van Rosmalen, M. M., Krom, M., & Merkx, M. (2017). Tuning the Flexibility of Glycine-Serine Linkers To Allow Rational Design of Multidomain Proteins. Biochemistry, 56(50), 6565–6574. https://doi.org/10.1021/acs.biochem.7b00902