Triose Phosphate Isomerase: Difference between revisions

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{{STRUCTURE_2ypi| PDB=2ypi | SCENE=Triose_Phosphate_Isomerase/Conserved/1}}  
{{STRUCTURE_2ypi| PDB=2ypi | SCENE=Triose_Phosphate_Isomerase/Conserved/1}}  


[[Image:loopsequence.jpg|left|thumb|200px|'''Loop 6 & 7 Sequence Homology'''.I.Kursula ''et al'' ''Protein Engineering, Design & Selection'' vol. 17 no.4 pp. 375-382, 2004]]
[[Image:loopsequence.jpg|left|thumb|250px|'''Loop 6 & 7 Sequence Homology'''.I.Kursula ''et al'' ''Protein Engineering, Design & Selection'' vol. 17 no.4 pp. 375-382, 2004]]


 
Due to its role in the glycolysis, an essential process to many organisms, TPI has been isolated and crystallized from several species giving rise to extensive multiple alignment ''in silico'' experiments which subsequently provided <scene name='Triose_Phosphate_Isomerase/Conserved/1'>amino acid conservation structures</scene> of TPI. <ref>PMID:12403619</ref> Collectively, these tools have determined that TPI has a roughly 50% sequence conservation from bacteria to humans,<ref>PMID:8130194</ref> One specific example of sequence homology is that of loop 6 and loop 7 residues.
Due to its role in the glycolysis, an essential process to many organisms, TPI has been isolated and crystallized from several species giving rise to extensive multiple alignment ''in silico'' experiments which subsequently provided <scene name='Triose_Phosphate_Isomerase/Conserved/1'>amino acid conservation structures</scene> of TPI. <ref>PMID:12403619</ref> Collectively, these tools have determined that TPI has a roughly 50% sequence conservation from bacteria to humans,<ref>PMID:8130194</ref>


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