Flexible linker used to fuse two proteins.
Designed considering the flexibility and separation needed between our fused proteins.
Protein coding region for the generation of 9AA linker. The linker will be composed of 4 amino acids from the scars from using RFC25 standard and Serin/Glycin residues.
Protein coding region for the generation of 6/9/12/15AA linker. The linker will be composed of 4 amino acids from the scars from using RFC25 standard and Serin/Glycin residues.
Protein coding region for the generation of 12 linker. The linker will be composed of 4 amino acids from the scars from using RFC25 standard and Serin/Glycin residues.
Highly flexible 6 amino acid linker. Translates to gsgsgs. Codon-optimize for E. coli, yeast, mammalian.
* gene synthesis * codon optimized for E. coli
This is a 15 amino acid flexible peptide linker protein domain that is useful for creating functional fusion proteins. The linker is to be fused in frame in between two protein domains, separating the two domains so that they each retain original functions yet will be physically connected.
This sequence is meant to be translated between two different protein domains, so no start or stop codon is present.
The DNA came from K.D. Wittrup's lab at MIT, on the pCTCON plasmid used for yeast scFv surface display.
Long 10AA Fusion Protein Linker with Standard 25 Prefix/Suffix
Jim Rose, Alex Bina, Ben Alouidor, Brian Avison
This is the longest of the three fusion protein linkers created by the Penn State 2011 iGEM team. It encodes for the ten amino acids GENLYFQSGG and has a prefix and suffix compatible with assembly standard 25. It is used in one of the variants of our Fast-Fusion protein reporter system.
This part contains the AgeI and NgoMIV sites as part of it's prefix/suffix that allows it to be used in standard 25 assembly. This part was synthesized through PCR oligo synthesis methods using the following primers: Forward: TATTGAATTCGCGGCCGCTTCTAGATGGCCGGCggtgaaaatttgtattttcaa Reverse: AATACTGCAGCGGCCGCTACTAGTATTAACCGGTaccaccagattgaaaatacaaattttcacc
Patrick Argos, An investigation of oligopeptides linking domains in protein tertiary structures and possible candidates for general gene fusion, Journal of Molecular Biology, Volume 211, Issue 4, 20 February 1990, Pages 943-958, ISSN 0022-2836, DOI: 10.1016/0022-2836(90)90085-Z. (http://www.sciencedirect.com/science/article/pii/002228369090085Z) Ryoichi Arai,Hiroshi Ueda,Atsushi Kitayama,Noriho Kamiya,and Teruyuki Nagamune. Design of the linkers which effectively separate domains of a bifunctional fusion protein Protein Eng. (2001) 14(8): 529-532 doi:10.1093/protein/14.8.529
This part is a linker, it can be used to connect two parts and add additional space between these parts. That can be necessary to avoid interactions between these parts. The GSAT linker was create to connect our protein domains Fok_a and Fok_i to an function final construct.
Designed for the fusion of proteins or peptides via in frame cloning, according to RFC25.
Highly flexible 10 amino acid linker. Translates to [GS]_5. Codon-optimize for E. coli, yeast, mammalian.
* gene synthesis * codon optimized for E. coli * experimental distance distributions are described in Neuweiler et al. 2006 papers.
(EAAAR)4 peptide linker, rigid; alpha helix secondary structure; see Yan et al. 2007
This a flexible linker combined by two former linkers, which can be easily connect to the end of protein with overlap pcr.
when we chose a linker for our fusion protein，we would have wanted to use -gggsgggs- linker. But we found that such a tandem repeating linker is hard to work well with overlap PCR because the OE region should be unique. Therefore, we improved the original part by change the first GGGS to a carefully selected natural linker from linker database to avoid repeating sequence. Besides, we used the selected natural linker to adjust its length to about 50A.
Highly flexible 2 aa linker. Translates to GS. Codon-optimal for E. coli, yeast, mammalian.
This linker was used to connect two different parts. The sequence produced the aminoacids Gly-Gly-Ser-Gly.
Oligos synthesized by sigma. Hybridized by PCR.
This part is a linker, it can be used to connect two parts and add additional space between these parts. That can be necessary to avoid interactions between these parts. We used this part to connect our protein domains with our lipocalin domains, for our project the universal endonuclease.The sequence produced the aminoacids Gly-Gly-Ser-Gly-Gly-Gly-Ser-Gly-Gly-Gly-Ser-Gly.
This part is a linker, it can be used to connect two parts and add additional space between these parts. That can be necessary to avoid interactions between these parts. We used this part to connect our protein domains with our lipocalin domains, for our project the universal endonuclease.The sequence produced the aminoacids Gly-Gly-Ser-Gly-Gly-Gly-Ser-Gly .
This part is a linker, it can be used to connect two parts and add additional space between these parts. That can be necessary to avoid interactions between these parts. The SEG linker was create to connect our protein domains Fok_a and Fok_i to an function final construct.
Designed for the fusion of proteins or peptides via in frame cloning, according to RFC25
15 aa flexible glycine-serine protein domain linker; Freiburg standard
A flexible, 15 aa long linker designed for fusion to/of proteins or peptides via in frame cloning. Consists of Glycine and Serine only.
Between BioBrick 1.0 sites this part is flanked 5' by NgoMI(=NgoMIV) and 3' AgeI(=PinAI) to facilitate in frame cloning for protein fusions.
Gene synthesis by ATG:biosynthetics, optimized for expression in homo sapiens by iGEM-Team Freiburg 2008
Short Fusion Protein Linker: GGSG with standard 25 prefix/suffix
This is the shortest of the three fusion protein linkers created by the Penn State 2011 iGEM team. It encodes for the four amino acids GGSG and has a prefix and suffix compatible with assembly standard 25. It is used in one of the variants of our Fast-Fusion protein reporter system.
This part contains the AgeI and NgoMIV sites as part of it's prefix/suffix that allows it to be used in standard 25 assembly. This part was synthesized through PCR oligo synthesis methods using the following primers: Forward (57.78 degrees) TATTGAATTCGCGGCCGCTTCTAGATGGCCGGCggtggttctggtACC Reverse (57.78 degrees) AATACTGCAGCGGCCGCTACTAGTATTAACCGGTaccagaaccaccG
Medium 6AA Fusion Protein Linker: GGSGGS with Standard 25 Prefix/Suffix
This is the mid-sized linker of the three fusion protein linkers created by the Penn State 2011 iGEM team. It encodes for the six amino acids GGSGGS and has a prefix and suffix compatible with assembly standard 25. It is used in one of the variants of our Fast-Fusion protein reporter system.
This part contains the AgeI and NgoMIV sites as part of it's prefix/suffix that allows it to be used in standard 25 assembly. This part was synthesized through PCR oligo synthesis methods using the following primers: Forward: 5??? TATTGAATTCGCGGCCGCTTCTAGATGGCCGGCggaggttcagg 3??? Reverse: 5???AATACTGCAGCGGCCGCTACTAGTATTAACCGGTgctgcctcctgaacctccGC 3'
The inspiration for this part came from the linker used in the 2010 Imperial College London iGEM team GFP-Xyle fusion part: BBa_K316007 Other Sources: Patrick Argos, An investigation of oligopeptides linking domains in protein tertiary structures and possible candidates for general gene fusion, Journal of Molecular Biology, Volume 211, Issue 4, 20 February 1990, Pages 943-958, ISSN 0022-2836, DOI: 10.1016/0022-2836(90)90085-Z. (http://www.sciencedirect.com/science/article/pii/002228369090085Z) Ryoichi Arai,Hiroshi Ueda,Atsushi Kitayama,Noriho Kamiya,and Teruyuki Nagamune. Design of the linkers which effectively separate domains of a bifunctional fusion protein Protein Eng. (2001) 14(8): 529-532 doi:10.1093/protein/14.8.529
Split fluorophore linker; Freiburg standard
Originally, this linker was used for fusion to the N-terminus of the C-terminal half of split fluorophores: Protein interactions can be examined by BiFC[1] using complementary, non-fluorescent fragments of fluorophores[2]. Therefore, it is essential that the C-terminal fragment of the fluorophore is not restricted too much in its mobility. The linker allows orientation and adaption of the C-terminal fragment to the N-terminal fragment of the split fluorophore and, thus, the reassembly of a working fluorescent protein. It has already been used in BiFC assays and is known to serve this purpose well[3]; anyway, another, more flexible linker that could be used instead is our ???GGGGS-linker??? (Part Bba_K157010).References see "Part Design".
This is a 10 amino acides long linker peptide which can be used to join protein domains together in a flexible way. So fusion proteins with variable DNA-binding and activation or repression domains might be assembled. <br\n>
To enable the fusion with other domains in frame the vector of this BioBrick has no base pair in between the restriction side and the BioBrick. Furthermore, this coding sequence does not include a start codon.<br\n> For more information about this issus, see:<br\n> Phillips, I.E. and Silver, P.A. "A new Biobrick Assembly Strategy Designed for Facile Protein Engineering." <br\n> DSpace http://hdl.handle.net/1721.1/32535 (2006).
Oligos with a yeast optimized coding for the peptide GENLYFQSGG have been ordered <br\n> The amino acide sequence corresponds to the interdomaine linker of xxx. ''paper''
This is a 40-50A flexible separation for fusion domains with a SV40 NLS, and its codon is optimized for mammalian. It can be used to link different protein domains for fusion proteins locating in cell nucleus.
The codon is optimized for mammalian, and we insert a NLS to promote locating in cell nucleus. Besides ,we lengthen this linker to provide better separation of two domains. At last we avoid tandem repeat sequence(like GGGSPKKKRKVGGGS), which will facilitate fusing this linker to your domains via overlap PCR.
This part is improved from BBa_K1486003.