Titin: Difference between revisions

As seen in the image (Z1Z2 / Telethonin complex), the major force enduring component of this complex is an elaborate intermolecular hydrogen bonding network formed across <scene name='2a38/Test/2'>β-strand</scene> among telethonin and Z1Z2 domains, and not intramolecularly among termini β-strands of individual Z1 or Z2 domains. This shift to a stronger force enduring interface reduces the possibility of unraveling the individual Ig-domains, thus stabilizing the complex. This demonstrates how <scene name='2a38/Test/2'>β-strand</scene> cross-linking via [http://en.wikipedia.org/wiki/Hydrogen_bonds hydrogen bonds] serves as an important mechanism. It functions as a molecular adhesive, increasing the ability of protein complexes to resist against mechanical stress.

== 3D Structures of Titin ==

[[4qeg]], [[5jdj]] - hTTN I10 residues 2880-2967<br />

[[1tit]], [[1tiu]]- hTTN I27 residues 5253-5341 – NMR<br />

[[5joe]] - hTTN I81 residues 9582-9671<br />

[[2rq8]] – hTTN residues 12677-12765 (mutant) – NMR<br />

[[1waa]] - hTTN residues 12801-12889<br />

[[1nct]], [[1ncu]] – hTTN M5 residues 26059-26155 – NMR<br />

[[1tnm]], [[1tnn]] – hTTN M5 residues 26059-26155<br />

[[3lcy]] – hTTN A164-A165 residues 31456-31649<br />

[[2nzi]] – hTTN residues 31854-32155<br />

[[3b43]] - rTTN I65-I70<br />

[[1h8b]] – rTTN residues 648-698 + hα Actinin 2 EF hands 3&4<br />

[[6i0y]] – TTN I27 residues 14318-14406 in 50S ribosome – ''Escherichia coli'' – Cryo EM<br />

==Additional Resources==