curbano's blog

I was a little surprised to see that 64% of the public supports the use of gene editing for both somatic and germline cells for therapeutic purposes but not for enhancement. I feel like most of the public don’t fully understand how genetics works in general, especially how gene editing would work. I appreciate that there are several regulatory organizations to help inform the public as well as figure out how to regulate gene editing, but what do they share with the public and how do we know these organizatons will make the best choices for everyone involved? Ethically, I feel like the use of somatic genome editing is better than germ-line genome editing becaue you can get consent from the person getting their genome edited. With germ-line gene editing, it is within the embryo, which cannot speak for itself and there is also a high risk to benefit ratio. Additionally, I am curious to know how a germ-line genome edited individual would reproduce and pass down their genes. I feel like the process of replication and passing down genes may be affected or harmed from genome editing.

The ability to change both our somatic and germ-line genomes is a very powerful tool for the human race. With this powerful tool also comes a lot of responsibility and questions on when it is acceptable to use and what is considered good or bad when gene editing. Gene therapy can definitely be abused and be dangerous if this power to change genomes is put into the wrong hands. I can see many different ways in which genome editing could go wrong and become harmful/abused. When genome editing was first introduced, I don’t think anyone really thought it would get to where it is now. It has already brought up so many ethical questions regarding natural selection, consent, disease treatment and more. I can imagine nations using genome editing to try to intentionally develop a virus/disease for warfare. Just like any new treatment such as a drug or method, there must be trials and tests carried out in order to confirm that is is safe and effective. Unfortunately, many companies are rushed due to patent applications and can lead to complications and harmful outcomes when testing. Additionally, it is difficult to fully test and know exactly what the effects of genome editing are. It seems like it would be difficult to find volunteers willing to be involved in these tests and it would be very expensive to carry out this research. I think with time, though, scientsists will be figure out ways to determine the effects of genome editing in order to make gene therapy as safe and effective as possible.

To remember the difference between discrete and continuous variables, I think of discrete as black and white and I think of continuous variables like a gray scale. probability is on a scale from 0-1. The closer a probability is to 1, the more likely it is to occur. Probability can be very helpful in many different topics, such as statistics. I don't know how probability will apply to physics, but I am curious to find out. Gibbs Free energy gives us information about a reaction. A positive Gibbs free energy means it is a non spontaneous reaction and requires energy to be put in for it to occur. A negative Gibbs free energy indicates that it is a spontaneous, or exothermic reaction and releases energy. To remember the difference between microstate and macrostate, micro is more specific and involves the specific make up or order of a system. The macrostate is the bigger picture, so it is the overall makeup or ratio of a system. Because of this, several different microstates can make the same macrostate.  A large number of particles is a very relative term. I looked it up and didn't find anything that defined what a large number of particles is. I, however, would assume it would be closer to infinity. Since one mole has about 6.022e23 molecules in it, I would assume you would need many more moles/molecules to have a large number of particles.

Proteins help with basically every function our body carries out. Our body is essentially made of cells and proteins. Proteins help build and repair tissue, make enzymes and hormones, as well as interact with one another to carry out even more complex cell processes. Additionally, a high Kd value indicates a low affinity. It's kind of like how a low pH value means a higher concentration of H+ ions. It's inversely proportional. A lot of factors can influence protein interaction. In class, I remember talking about several factors. We mentioned how heat, light, pH, detergent, etc can influence the non covalent bonds in proteins. I am wondering if there are any things that can influence the interaction of covalent bonds.

Like many systems and things in our bodies, many proteins work together to carry out certain functions. If one protein in a certain system or group is misfolded, it may cause a chain reaction of errors to appear in the entire system. Studying the interactions between certain proteins can help us better understand how certain interactions operate as well as think of ways to possible fix certain malfunctions. I think this sentence is trying to tell us that there is a variety of ways these complexes can come together. I don't think identical complexes work better or worse than different complexes, it just depends what the protein complex's function is overall. It's like when we look at subunits in quaternary proteins. Some subunits can be the same within the protein, while sometimes they are different. I think this sentence is trying to tell us that there is a variety of ways these complexes can come together. I don't think identical complexes work better or worse than different complexes, it just depends what the protein complex's function is overall. It's like when we look at subunits in quaternary proteins. Some subunits can be the same within the protein, while sometimes they are different.

This makes sense since most amino acids have no charge at all or very little charge. The less stable something is, the more energy it will use. The hydrophobic amino acids often are folded into the middle of the final protein structure to avoid instability. Chaperone cells are meant to assist with protein folding to make sure the protein folds into their correct shape. However, sometimes the up regulation or down regulation of these cells can cause the structure to not be folder properly. I'd expect to see more hydrophobic amino acids exposed when there's down regulation of chaperone cells. Is there an enzyme or drug that can be used to help control the regulation? From the reading, I took away that in the dominant-negative mechanism, the mutant protein is either dominant or co dominant to the wild type dominant protein. This causes the mutant protein to influence the function of the wild type dominant protein "negatively," or decreases its function. The mutant protein may completely take control over the dominant protein, or it may just decrease the dominant protein's activity. Proteins play a vital role in the way our bodies function and perform. After reading this article, it showed me how even a slight error or mutation can cause a lot of issues and cause diseases to form. Finding ways to help proteins conform to their proper shape can help cure many diseases. Understanding each level of protein structure is vital when finding cures to certain diseases and finding ways to manipulate protein shape to the correct conformation.

While they seem nearly identical, they are actually quite different. If you tried to place the L amino acid on top of the D amino acid, it would be impossible for them to line up the same way. This leads to their interaction with other molecules to be different from one another. Online I found that it is still not fully known why D amino acids are so rare, but found it is manly because L amino acids tend to be more successful in nature for some reason. A cross link is a bond that links one polymer chain to another. Examples of this can be covalent bonds or ionic bonds. Here, with proteins, it would be the peptide bonds. A cross link is a bond that links one polymer chain to another. Examples of this can be covalent bonds or ionic bonds. Here, with proteins, it would be the peptide bonds. I find it surprising yet interesting that ion pairs between N and C groups as well as strong disulfide bonds and hydrogen bonding don't contribute much to the stability of a protein. Disulfide bonds are one of the strongest bonds so I would think that bonding would help stabilize the protein. However, structures and ions such as zinc are more important with helping with the stability of a protein.

SH3 and SH2 domains play a large role in many signal pathways. It is a binding site for proteins with phosphorylated tyrosine. By the name auto inhibition, I would assume the protein itself is able to inactivate itself. I am curious to know how this system works exactly, though. I wonder if the protein receives a signal? These are common pathways that was addressed in class. There are 3 proteins that are needed for the activation of this pathway. If there is a mutation that influences the function of one of these proteins, the enter pathway is affected. Is there a way for the pathway to compensate for a mutation in one of these proteins? If so, how does that work? Grb2 is a growth factor receptor-bound protein. It is a big player is many signal transduction pathways and cell communication.

In every living organism, structure plays a large role in the function of certain things. Proteins make up nearly all living organisms, so understanding the structure of proteins can help us understand the overall structure and function of us and other living things. Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. Primary structure is the sequence of amino acids, which are linked together with peptide bonds. Secondary structure are structures the sequence of amino acids often form into. Proteins usually have alpha helices and/or beta sheets. Alpha helices are helices, similar to the structure of DNA. Beta sheets are flat structures that can run parallel or antiparallel. Usually, the two middle sheets are parallel and the two sheets on the outside are antiparallel to those. The bonding that is involved in secondary structure is hydrogen bonding Tertiary structure is the overall fold of a single polypeptide chain. Quaternary structure is the folding of two or more polypeptide chains, subunits, that function together. The bonds that are involved in tertiary/quaternary structure are the noncovalent bonds.

In nearly every living species, temperature influences physiological and biological processes in the body. Spiders are ectothermic organisms, meaning they are unable to regulate their body temperatures relative to their environment. Because of this, changes in temperature can have a large impact on their metabolic rate and overall activity (Barghusen et al). It has been found that even winter active spiders will make less effective webs or no webs at all at temperatures 2° colder than the temperature they are accustomed to. Having a less effective, or no, web greatly reduced feeding, which could be detrimental for spiders (Aitchison 1984). Since web production is a large part of spider activity and survival, we decided to focus our project on how varying temperatures influence web production. Past research has found that spiders in lower temperatures tend to use less spiral silk than spiders in warmer temperatures (Vollrath et al). Our project focuses on how temperature influence the weight of webs.