https://padlet.com/dhouse22/3AProteins To complete this padlet, refer to the directions here: https://docs.google.com/document/d/1qMormESiHeBN76tRSRC6mkxe1r2DKflj-GG_bzgCXGo/edit?usp=sharing en-us 2019-02-01 07:58:50 UTC 2025-12-06 12:38:01 UTC hello@padlet.com https://padlet.com/dhouse22/3AProteins/wish/327944966 It caused for the protein to become more tightly coiled because the structure became more complex
2. The sequence changing caused the function to change]]> 2019-02-05 18:30:31 UTC https://padlet.com/dhouse22/3AProteins/wish/327944966 https://padlet.com/dhouse22/3AProteins/wish/327945434 Q1. Affecting the amino acid sequence on the model by adding another red bead in place of a yellow bead caused the end of the sequence to double back and be closer to the blue bead. This causes the structure to be more complex and tightly structured.
2.  Changing the structure of the beads brought in another charge to be present and thusly the lysosome would be introduced to challenges in the transportation of materials.]]> 2019-02-05 18:31:17 UTC https://padlet.com/dhouse22/3AProteins/wish/327945434 https://padlet.com/dhouse22/3AProteins/wish/327945797 1. Changing the amino acid structure caused the protein model to be more compact since there are two reed beads being attracted to single blue bead which adds to the complexity of the structure
2. The change i the structure would cause the model to be unbalanced and it would not be able to function properly  ]]> 2019-02-05 18:31:52 UTC https://padlet.com/dhouse22/3AProteins/wish/327945797 https://padlet.com/dhouse22/3AProteins/wish/327946088 1. Changing the amino acid sequence (removing a yellow bead and adding another red bead) caused the protein to become more compact. The protein model now has two red beads attracted to one blue bead, so it's tighter in the center.
2. A change in the sequence of an amino acid can cause a change in the function and structure of its protein (in a negative way). If the protein is not able to function properly, lysosomes can have a hard time transporting and/or breaking down materials like Glycogen (which, if in excess, can cause swelling and weak muscles) in the body. ]]> 2019-02-05 18:32:17 UTC https://padlet.com/dhouse22/3AProteins/wish/327946088 https://padlet.com/dhouse22/3AProteins/wish/327949397 Q1 - Changing the amino acid sequence changed the way the amino acids interacted and changed the shape of the protein.

Q2 - The change in amino acid placement causes an imbalance in the structure of the protein, likely to cause it not to function properly.]]> 2019-02-05 18:37:13 UTC https://padlet.com/dhouse22/3AProteins/wish/327949397 https://padlet.com/dhouse22/3AProteins/wish/327949654 1. Changing the amino acid changed the structure of the protein model, making it more tightly compact in the center of the folding. Because there now are two red amino acids attracting to a single blue amino acid, the folding is now tighter together in the middle. 
2. The change in the amino acid placement results in a change in the structure and function of the protein. Because of mutations like this, diseases like Pompe occur, as glycogen is unable to be broken down and causes swelling and bad reactions within the body. ]]> 2019-02-05 18:37:34 UTC https://padlet.com/dhouse22/3AProteins/wish/327949654 https://padlet.com/dhouse22/3AProteins/wish/327950341 1. Changing the amino acid sequence caused the structure of the protein model to become much less compact and the red and blue beads would ultimately not be able to stay as tightly together than the original model. The change in beads ultimately complicated the folding process
2. The change in beads would create an imbalance in charges and with the clusters of hydrophobic and hydrophilic beads being thrown off, it could make it difficult for lysosomes to transport materials ]]> 2019-02-05 18:38:37 UTC https://padlet.com/dhouse22/3AProteins/wish/327950341 https://padlet.com/dhouse22/3AProteins/wish/327950974 Q1 - changing the amino acid sequence caused the structure of the protein model to be further apart because there is an other red in the second sequence and so it created a different shape in the protein and caused it to be folded differently
Q2 - Changing the beads created another charge to be present and therefore the lysosomes couldn't provide transportation as easily and it causes an imbalance.]]> 2019-02-05 18:39:30 UTC https://padlet.com/dhouse22/3AProteins/wish/327950974 https://padlet.com/dhouse22/3AProteins/wish/327951742 1. Altering the amino acid caused the structure or shape of the amino acid to change. It also changed how to amino acids interacted after we were instructed to remove certain colored beads and replace them with others.
2. This would cause the balance to be unequal which would result in the proteins not functioning regularly.]]> 2019-02-05 18:40:34 UTC https://padlet.com/dhouse22/3AProteins/wish/327951742 https://padlet.com/dhouse22/3AProteins/wish/327953785 1.  After changing the amino acid, it changed the shape of the proteins and it also altered the interaction between them as well. One of the red beads didn't have a blue bead to bond with so they were connected to opposite ends of the one blue bead I had.
2.  The change in enzyme functions would cause the proteins not to function properly because it would be unbalanced.]]> 2019-02-05 18:42:53 UTC https://padlet.com/dhouse22/3AProteins/wish/327953785 10024492 https://padlet.com/dhouse22/3AProteins/wish/327954986 1. When the amino acid sequence was changed, it effected how the beads folded since they interacted differently with each other due to the change in sequence. With the addition of another yellow bead, another fold was created for it to go to the center.
2.  Glycogen cannot be digested by lysosomes. Ergo, glycogen builds up in the lysosomes to the point where the cell can be ruined.]]> 2019-02-05 18:44:33 UTC https://padlet.com/dhouse22/3AProteins/wish/327954986 https://padlet.com/dhouse22/3AProteins/wish/327955171 1. Changing the amino acid changed the structure of the protein model by making it more compact as there are two red beads trying to come closer to the blue bead. The change in beads made the folding more complex. 
2. The change in enzyme function could be mirrored to a DNA mutation that changed the sequence of amino acids in GAA. This mutation inhibits glycogen from being broken down by the lysosomes. Thus like in the case of Pompe disease, there is a build up of glycogen.]]> 2019-02-05 18:44:45 UTC https://padlet.com/dhouse22/3AProteins/wish/327955171 10039421 https://padlet.com/dhouse22/3AProteins/wish/327958299 1.  When the amino acid was changed, it changed the shape of the protein and how it interacted.  The red bead doesn't have a blue to bond with.  
2. Glycogen is unable to be broken up in the lysosome. The causes a build up of glycogen. The lysosome grows larger and larger, and the function of the cell is at risk. ]]> 2019-02-05 18:48:51 UTC https://padlet.com/dhouse22/3AProteins/wish/327958299