Difference between revisions of "Part:BBa K1486004"

 
Line 5: Line 5:
 
Flexible linker used to fuse two proteins.
 
Flexible linker used to fuse two proteins.
  
−
<!-- Add more about the biology of this part here
+
 
 
===Usage and Biology===
 
===Usage and Biology===
 +
This linker is part of the group of flexible ligands composed of small, non-polar amino acids such as Gly and polar such as Ser. In this way, they guarantee high mobility and offer flexibility for the functional domains of connection. Studies show that when proline residues are exchanged in place of terminal glycine residues, degrees of independence are lost (Ruiz et al., 2016b). In this way, enzyme activity is decreased, which leads to low catalytic efficiencies. We can conclude that flexible ligands provide a reduced catalytic activity for proteins.
 +
        The article “Linkers: a synergistic way for chimeric proteins, 2020”, talks about the constitution and interaction of the flexible linker (Gly-Gly-Gly-Gly-Ser)n, where “n” specifies the sum of the repetitions of the residue. These linkers provide partial domain separation. It is possible to observe that the amount of Gly, Ser and Thr residues results in flexibility that allows the
 +
mobility of the functional binding domains.
 +
 +
  
−
<!-- -->
 
 
<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
 
<partinfo>BBa_K1486004 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K1486004 SequenceAndFeatures</partinfo>
  
  
−
<!-- Uncomment this to enable Functional Parameter display
+
 
 
===Functional Parameters===
 
===Functional Parameters===
 
<partinfo>BBa_K1486004 parameters</partinfo>
 
<partinfo>BBa_K1486004 parameters</partinfo>
 +
Isoelectric Point: 5,52
 +
Molecular Weight: 648,59Da
 
<!-- -->
 
<!-- -->
 +
===References===
 +
#Michela S, Baenziger-Tobler N, Wibke L, Sarah B, Julian B, Dragan G. Linker Length Matters, Fynomer-Fc Fusion with an Optimized Linker Displaying Picomolar IL-17A Inhibition Potency. IMMUNOLOGY| VOLUME 289, ISSUE 20, P14392-14398, MAY 2014

Revision as of 08:26, 21 October 2021


flexible linker 2x (GGGGS)

Flexible linker used to fuse two proteins.


Usage and Biology

This linker is part of the group of flexible ligands composed of small, non-polar amino acids such as Gly and polar such as Ser. In this way, they guarantee high mobility and offer flexibility for the functional domains of connection. Studies show that when proline residues are exchanged in place of terminal glycine residues, degrees of independence are lost (Ruiz et al., 2016b). In this way, enzyme activity is decreased, which leads to low catalytic efficiencies. We can conclude that flexible ligands provide a reduced catalytic activity for proteins. 

       	The article “Linkers: a synergistic way for chimeric proteins, 2020”, talks about the constitution and interaction of the flexible linker (Gly-Gly-Gly-Gly-Ser)n, where “n” specifies the sum of the repetitions of the residue. These linkers provide partial domain separation. It is possible to observe that the amount of Gly, Ser and Thr residues results in flexibility that allows the

mobility of the functional binding domains.


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Functional Parameters

chassisE coli
device_typelinker
directionforward

Isoelectric Point: 5,52 Molecular Weight: 648,59Da

References

  1. Michela S, Baenziger-Tobler N, Wibke L, Sarah B, Julian B, Dragan G. Linker Length Matters, Fynomer-Fc Fusion with an Optimized Linker Displaying Picomolar IL-17A Inhibition Potency. IMMUNOLOGY| VOLUME 289, ISSUE 20, P14392-14398, MAY 2014