Ubiquitin Structure & Function: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 6: | Line 6: | ||
Ubiquitin can not only be found in the nucleus, but in the cytoplasm and cell-surface membrane as well. | Ubiquitin can not only be found in the nucleus, but in the cytoplasm and cell-surface membrane as well. | ||
One interesting characteristic of ubiquitin is its stability. Ubiquitin is able to withstand a range of pH levels and temperatures and is very resistant to tryptic digestion, while still containing seven Lysine and four arginine residues. Many aspects of ubiquitin's structure aid in this durability. Ubiquitin contains a hydrophobic core. Three hydrophobic residues found on the α-helix and 11 of the 13 hydrophobic residues from the β-sheet are involved in constructing this hydrophobic core. The main contributor to the ubiquitin stability is the vast amount of hydrogen-bonding interactions observed. The whole structure of ubiquitin undergoes significant hydrogen bonding, aside from the COOH terminus. | One interesting characteristic of ubiquitin is its stability. Ubiquitin is able to withstand a range of pH levels and temperatures and is very resistant to tryptic digestion, while still containing seven Lysine and four arginine residues. Many aspects of ubiquitin's structure aid in this durability. Ubiquitin contains a hydrophobic core. Three hydrophobic residues found on the α-helix and 11 of the 13 hydrophobic residues from the β-sheet are involved in constructing this hydrophobic core. The main contributor to the ubiquitin stability is the vast amount of hydrogen-bonding interactions observed. The whole structure of ubiquitin undergoes significant hydrogen bonding, aside from the COOH terminus. | ||
[[Image:lysubq.png|500 px|center]] | |||
[[Image:1ubiq.png|300 px|right]] | [[Image:1ubiq.png|300 px|right]] | ||
=Function= | =Function= | ||
