[2-3] Cloning

What are some of the social challenges a 


cloned child might face?

A cloned child will face a lot of problems. Especially since a clone is very liable to develop feelings.
Feelings are a very powerful thing, though many would not consider it science.
Of course, plants are okay to clone because plants benefit everyone, for food and oxygen. The more plants, the better (but not too much or else there will be a plant apocalypse).
Maybe cloning animals are okay, too. Because it can help make more endangered animals, and more source of food.


Cloning humans, I believe, is extremely dangerous. And yes, basically for the sappy reasons like feelings&emotions. If I were a clone and I realized I was merely a creation of science, and not love, I don't know how I would cope. Here is a brief overview of how I imagine a cloned child to grow up:


Childhood: The clone has no parents, unless it's original human form was considered a human. Growing up without parents is a tragedy. If someone made a clone of me, why would I hang around it? Even if I did, how am I supposed to take care of it? Welfare or something? This is not my baby; this is science and there is no love. It would be very difficult for the clone to make friends, too. Since a clone has it's original form existing with it, peers would have a hard time accepting the clone, probably being freaked out.


Adolescent: It is never guaranteed that a clone would come out perfect. Hormonal problems may occur. On the other hand, if there are no hormonal problems, the clone would be very lonely. Since adolescent is the period of time in which teens become more emotional, the clone would be that to the highest extent. No parents, no friends, probably only the scientist who created it would probably care for it. It might commit suicide from sadness. But if not...


Adult: The clone would probably be very sexually frustrated. I don't think much people would want to date or marry someone if they knew he or she was a clone. Since having babies might be a concern for many adults, they would not opt for a clone as a parent; problems with it's birth may occur. It is not safe. 


I am very much against cloning. I think cloning is basically science vs. nature. You should not fight against the way things have sufficiently worked for centuries. Who would want to be cloned anyway? Why would anyone want a copy of themselves out there? Even when someone wears the same shirt as you, people get worked up. Cloning humans will do us no good, in my opinion.

[BOW 2-2] Mutations.

I think this is photoshopped...

SENSE: Sense mutations occur among the bases that code for amino acids. They could be beneficial for disastrous.


NON-SENSE: This mutation that changes a codon to a stop codon, which results in a shorter and typically nonfunctional protein.


DELETION: Deletion is the loss of genetic substances. Any number of nucleotides can be deleted. Deletion can cause a frame-shift.


INSERTION: This is the addition of one or more nucleotide base pairs into a DNA sequence. Insertions range from anywhere in size.


FRAME-SHIFT: When the number of nucleotides are not divisible by 3, a frame-shift is caused. This is typically caused by deletions and insertions.


POINT: A single base is substituted for another. This changes the meaning of a codon, leaving the rest of the gene untouched.


TRANS-LOCATION: When a part of a gene gets placed at a different spot than its designation, a trans-location mutation takes place. This doesn't only cause mutations, but can also cause diseases and cancer.




References:
http://student.ccbcmd.edu/~gkaiser/biotutorials/protsyn/mutate.html
http://en.wikipedia.org/wiki/Insertion_%28genetics%29

[BOW 2-1] Translation!

The three steps of tranlsation are initiation, elongation, and termination.

Initiation-- An mRNA joins to the small ribosomal unit at the 5' end region that has not been translated yet. The large ribosomal subunit attaches to the small subunit so that the firat codon is in line with the P building site. A tRNA that is carrrying the amino acid methionine attaches to the start codon (AUG) on the mRNA, which initiates elongation.

Elongation-- Attachment of first amino acid carries tRNA to A binding site. A tRNA and its amino acid attaches to the same A binding site. A peptide bond forms between the methionine and the amino acid carried at the A building site. Ribosome now moves towards in the 3' direction down the mRNA by three bases, or by one codon shifting the tRNA and polypeptide chain to the P binding site.

tRNA is then ejected from the E building region.

Elongation repeats until a stop codon is encountered.

Termination-- The polypeptide chain is now at the P site, and the stop codon is at the A site. A protein attaches to the stop codon at the A building site. This protein initiates separation in the polypeptide chain, which then goes into the cytoplasm.

References:

http://en.wikipedia.org/wiki/File:Ribosome_mRNA_translation_en.svg

http://answers.yahoo.com/question/index?qid=20080512231434AApX9GU

http://staff.jccc.net/pdecell/proteinsynthesis/translation/steps.html

[BOW] Extra Credit

What topics really confused you?

Photosynthesis and meiosis were difficult for me to understand for me.

What topics do you feel very clear on?

Viruses, macromolecules, cell structure, atoms, and nutrition were pretty clear and interesting topics.

What lab/ activity was your favorite? Why?
I liked the genetics lab and sex lab because the instructions were simple and fun. I liked drawing my "child", hehe.

What lab/activity was your least favorite? Why?

The labs with microscopes like bacteria/yogurt lab and pond water lab were kind of hard. It takes a while for me to work the microscope to see the image clearly.

If you could change something about the class to make it better, for instance the type of homework (not the amount) what would it be and why?

Hmmmm.... i don't know. I think the way the class works is fine.

Blast Gene WS

Gene Sequence 2
This gene encodes a protein that is one of the two components of elastic fibers. The encoded protein is rich in hydrophobic amino acids such as glycine and proline, which form mobile hydrophobic regions bounded by crosslinks between lysine residues. Deletions and mutations in this gene are associated with supravalvular aortic stenosis (SVAS) and autosomal dominant cutis laxa. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]


Gene Sequence 3
Alzheimer's disease (AD) patients with an inherited form of the disease carry mutations in the presenilin proteins (PSEN1 or PSEN2) or the amyloid precursor protein (APP). These disease-linked mutations result in increased production of the longer form of amyloid-beta (main component of amyloid deposits found in AD brains). Presenilins are postulated to regulate APP processing through their effects on gamma-secretase, an enzyme that cleaves APP. Also, it is thought that the presenilins are involved in the cleavage of the Notch receptor such that, they either directly regulate gamma-secretase activity, or themselves act are protease enzymes. Two alternatively spliced transcript variants encoding different isoforms of PSEN2 have been identified. [provided by RefSeq, Jul 2008]


Gene Sequence 5
This gene encodes a member of the fibrillin family. The encoded protein is a large, extracellular matrix glycoprotein that serve as a structural component of 10-12 nm calcium-binding microfibrils. These microfibrils provide force bearing structural support in elastic and nonelastic connective tissue throughout the body. Mutations in this gene are associated with Marfan syndrome, isolated ectopia lentis, autosomal dominant Weill-Marchesani syndrome, MASS syndrome, and Shprintzen-Goldberg craniosynostosis syndrome. [provided by RefSeq, Jul 2008]


Gene Sequence 6
The protein encoded by this gene is a negative regulator of the cell cycle and was the first tumor suppressor gene found. The encoded protein also stabilizes constitutive heterochromatin to maintain the overall chromatin structure. The active, hypophosphorylated form of the protein binds transcription factor E2F1. Defects in this gene are a cause of childhood cancer retinoblastoma (RB), bladder cancer, and osteogenic sarcoma. [provided by RefSeq, Jul 2008]


Gene Sequence 8
The dystrophin gene is the largest gene found in nature, measuring 2.4 Mb. The gene was identified through a positional cloning approach, targeted at the isolation of the gene responsible for Duchenne (DMD) and Becker (BMD) Muscular Dystrophies. DMD is a recessive, fatal, X-linked disorder occurring at a frequency of about 1 in 3,500 new-born males. BMD is a milder allelic form. In general, DMD patients carry mutations which cause premature translation termination (nonsense or frame shift mutations), while in BMD patients dystrophin is reduced either in molecular weight (derived from in-frame deletions) or in expression level. The dystrophin gene is highly complex, containing at least eight independent, tissue-specific promoters and two polyA-addition sites. Furthermore, dystrophin RNA is differentially spliced, producing a range of different transcripts, encoding a large set of protein isoforms. Dystrophin (as encoded by the Dp427 transcripts) is a large, rod-like cytoskeletal protein which is found at the inner surface of muscle fibers. Dystrophin is part of the dystrophin-glycoprotein complex (DGC), which bridges the inner cytoskeleton (F-actin) and the extra-cellular matrix. [provided by RefSeq, Jul 2008]

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