Keratins: Difference between revisions
Deleted Fig. 1 and moved its caption to Fig. 3. The editing is to correct the page after the move to HTML5 standard that does not allow multiple applets on the page. |
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* Hydrogen bonds between suitable groups. | * Hydrogen bonds between suitable groups. | ||
In the 2B domains of keratins type I K14 and type II K5 shown in Fig. | In the 2B domains of keratins type I K14 and type II K5 shown in Fig. 2, there are two and a single cysteine respectively. These cysteines are far apart and cannot form disulfide bridges. | ||
* <scene name='55/559109/Cysteines/1'>Click here to see the locations of the Cys in Fig. | * <scene name='55/559109/Cysteines/1'>Click here to see the locations of the Cys in Fig. 2.</scene> (Wait a few moments for change of scene) | ||
Thus, disulfide bridges cannot be responsible for the binding of K14 and K5. | Thus, disulfide bridges cannot be responsible for the binding of K14 and K5. | ||
The second option is ionic bonds, or salt bridges between the two keratins. | The second option is ionic bonds, or salt bridges between the two keratins. | ||
* <scene name='55/559109/Acidic-residues/1'>Click here to see the acidic residues, Asp and Glu in Fig. | * <scene name='55/559109/Acidic-residues/1'>Click here to see the acidic residues, Asp and Glu in Fig. 2.</scene> | ||
* <scene name='55/559109/Basic-aas/1'>Click here to see the basic residues, Arg and Lys.</scene> | * <scene name='55/559109/Basic-aas/1'>Click here to see the basic residues, Arg and Lys.</scene> | ||
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===Hydrophobic residues: Main points of contact between chains === | ===Hydrophobic residues: Main points of contact between chains === | ||
The third option noted above is hydrophobic interactions between the two keratins. | The third option noted above is hydrophobic interactions between the two keratins. | ||
* <scene name='55/559109/Hydrophobic-aas/1'>Click here to see the hydrophobic residues in Fig. | * <scene name='55/559109/Hydrophobic-aas/1'>Click here to see the hydrophobic residues in Fig. 2.</scene> | ||
It can be seen that the hydrophobic residues are predominantly located in the interface between the two chains and essentially occupy the space between these chains. Thus, hydrophobic residues that can associate with one another in the aqueous environment of cell are the main points of contact between the chains in the coiled-coil. | It can be seen that the hydrophobic residues are predominantly located in the interface between the two chains and essentially occupy the space between these chains. Thus, hydrophobic residues that can associate with one another in the aqueous environment of cell are the main points of contact between the chains in the coiled-coil. | ||