In The Tube
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Thursday, February 23, 2012
Natural Selection! And I'm First Pick, Naturally!
Natural selection is the primary way that organisms become better adapted to their environment. It relates to phenotype since the animals who adapt to their environment have different personality. The animals each have different genes so that relates to genotypes. Finally some reproduction may have a mutation through each offspring. A exaptation is a change in the trait during evolution.
Cloning! Spooky!
If a clone originates from an existing person, who is the parent?
I believe the parent would be the person who's gene it came from. Since in a regular birth the child would have the same gene as there parents. Even if the outcome would be identical since it is a clone of the same genes, the person who's gene is in the clone should be the parent of the child.
http://www.google.com/imgres?q=clones&um=1&hl=en&safe=active&client=safari&sa=N&rls=en&biw=1278&bih=843&tbm=isch&tbnid=zOJv4iLso4UjaM:&imgrefurl=http://www.sodahead.com/living/lets-picture-an-scenario-if-human-cloning-was-legal-should-those-clones-be-treated-as-other-human/question-1957455/%3Fpage%3D7&docid=FPSZZdaSFOZO5M&imgurl=http://images.sodahead.com/polls/001957455/3752698267_human_cloning_answer_1_xlarge.jpeg&w=350&h=261&ei=HYNGT6e9Ms3WiALw__naDQ&zoom=1&iact=rc&dur=498&sig=106118596005183164299&page=1&tbnh=150&tbnw=201&start=0&ndsp=22&ved=1t:429,r:9,s:0&tx=140&ty=53&surl=1
Tuesday, February 7, 2012
Mutation! TMNT! Wahahaha!
Sense mutation- this is sometimes seen with a single substitution mutation when the change in the DNA base sequence results in a new codon that is still coding for the same amino acid. (All amino acids are coded for by more than one codon.)
frameshift mutation (also called a framing error or a reading frame shift) is a genetic mutation caused by indels (insertions or deletions) of a number of nucleotides that is not evenly divisible by three from a DNA sequence. Due to the triplet nature of gene expression by codons, the insertion or deletion can change the reading frame (the grouping of the codons), resulting in a completely different translation from the original. The earlier in the sequence the deletion or insertion occurs, the more altered the protein produced is.
Nonsense Mutations- the term "nonsense mutation is used because the stop codon has "no sense" for an amino acid. Nonsense mutations cause the protein to be cut off early and therefore incomplete, which usually renders it non-functional. Cystic fibrosis is a disease caused by a nonsense mutation.
Deletion Mutation- In genetics, a deletion (also called gene deletion, deficiency, or deletion mutation) (sign: Δ) is a mutation (a genetic aberration) in which a part of a chromosome or a sequence of DNA is missing. Deletion is the loss of genetic material. Any number of nucleotides can be deleted, from a single base to an entire piece of chromosome.[1] Deletions can be caused by errors in chromosomal crossover duringmeiosis. This causes several serious genetic diseases. Deletion also causes frameshift.
Insertion Mutation-In genetics, an insertion (also called an insertion mutation) is the addition of one or more nucleotide base pairs into a DNAsequence. This can often happen in microsatellite regions due to the DNA polymerase slipping. Insertions can be anywhere in size from one base pair incorrectly inserted into a DNA sequence to a section of one chromosome inserted into another.
On a chromosome level, an insertion refers to the insertion of a larger sequence into a chromosome. This can happen due to unequal crossover during meiosis.
&docid=-EJBB_BTrSrlPM&imgurl=http://upload.wikimedia.org/wikipedia/commons/thumb/0/06/Insertion-genetics.png/300px-Insertion-genetics.png&w=300&h=207&ei=pkU9T5reCOmRiQLTx-yLAQ&zoom=1&iact=rc&dur=323&sig=106118596005183164299&page=1&tbnh=150&tbnw=224&start=0&ndsp=20&ved=0CEkQrQMwAQ&tx=156&ty=31&surl=1){kind=link}
Point mutation-A point mutation, or single base substitution, is a type of mutation that causes the replacement of a single base nucleotidewith another nucleotide of the genetic material, DNA or RNA.
Translocation Mutation-n genetics , a chromosome translocation is a chromosome abnormally caused by rearrangement of parts between non humologous chromosomes a genes fusion .may be created when the translocation join two otherwise separate genes , the occurrence of which is common in cancer .
Thursday, February 2, 2012
Semester 2: BOW 1! YEAH!
Prior to the beginning of the protein synthesis, all of the component parts are assembled in the ribosome which is the brown/tan structure in the left graphic.
STEP 2: Initiation:
In the cytoplasm, protein synthesis is actually initiated by the AUG codon on mRNA. The AUG codon signals both the interaction of the ribosome with m-RNA and also the tRNA with the anticodons (UAC). The tRNA which initiates the protein synthesis has N-formyl-methionine attached. The formyl group is really formic acid converted to an amide using the -NH2 group on methionine (left most graphic)
The next step is for a second tRNA to approach the mRNA (codon - CCG). This is the code for proline. The anticodon of the proline tRNA which reads this is GGC. The final process is to start growing peptide chain by having amine of proline to bond to the carboxyl acid group of methinone (met) in order to elongate the peptide.
STEP 3: Elongation:
Elongation of the peptide begins as various tRNA's read the next codon. In the example on the left the next tRNA to read the mRNA is tyrosine. When the correct match with the anticodons of a tRNA has been found, the tyrosine forms a peptide bond with the growing peptide chain .
The proline is now hydrolyzed from the tRNA. The proline tRNA now moves away from the ribosome and back into the cytoplasm to reattach another proline amino acid.
Step 4: Elongation and Termination:
When the stop signal on mRNA is reached, the protein synthesis is terminated. The last amino acid is hydrolyzed from its t-RNA.
The peptide chain leaves the ribosome. The N-formyl-methionine that was used to initiate the protein synthesis is also hydrolyzed from the completed peptide at this time.
The ribosome is now ready to repeat the synthesis several more times.
Elongation of the peptide begins as various tRNA's read the next codon. In the example on the left the next tRNA to read the mRNA is tyrosine. When the correct match with the anticodons of a tRNA has been found, the tyrosine forms a peptide bond with the growing peptide chain .
The proline is now hydrolyzed from the tRNA. The proline tRNA now moves away from the ribosome and back into the cytoplasm to reattach another proline amino acid.
Step 4: Elongation and Termination:
When the stop signal on mRNA is reached, the protein synthesis is terminated. The last amino acid is hydrolyzed from its t-RNA.
The peptide chain leaves the ribosome. The N-formyl-methionine that was used to initiate the protein synthesis is also hydrolyzed from the completed peptide at this time.
The ribosome is now ready to repeat the synthesis several more times.
Extra! Extra! Get all the credit!
What topics really confused you?
The most confusing thing about biology is having to memorize over 15 terms a chapter, and all the terms are 8 letters long. Such as glycolisis, polypeptide, monosacharride, etc. (wrong spelling (x_x)!)
What topics do you feel very clear on?
I feel very confident in naming cell organelles and organelle functions; as well as naming different prokaryotes and eukaryotes
What lab/activity was your favorite? Why?
The song lab because making the rap was fun and I like work that pushes me to be creative.
What lab/activity was your least favorite? Why?
The microscope lab because I had the hardest time understanding that the most.
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?
More labs which involve drawing and music, because it's more fun.
The most confusing thing about biology is having to memorize over 15 terms a chapter, and all the terms are 8 letters long. Such as glycolisis, polypeptide, monosacharride, etc. (wrong spelling (x_x)!)
What topics do you feel very clear on?
I feel very confident in naming cell organelles and organelle functions; as well as naming different prokaryotes and eukaryotes
What lab/activity was your favorite? Why?
The song lab because making the rap was fun and I like work that pushes me to be creative.
What lab/activity was your least favorite? Why?
The microscope lab because I had the hardest time understanding that the most.
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?
More labs which involve drawing and music, because it's more fun.
Name that gene! Foo!
gene sequence 1:
Huntingtin is a disease gene linked to Huntington's disease, a neurodegenerative disorder characterized by loss of striatal neurons. This is thought to be caused by an expanded, unstable trinucleotide repeat in the huntingtin gene, which translates as a polyglutamine repeat in the protein product. A fairly broad range in the number of trinucleotide repeats has been identified in normal controls, and repeat numbers in excess of 40 have been described as pathological. The huntingtin locus is large, spanning 180 kb and consisting of 67 exons. The huntingtin gene is widely expressed and is required for normal development. It is expressed as 2 alternatively polyadenylated forms displaying different relative abundance in various fetal and adult tissues. The larger transcript is approximately 13.7 kb and is expressed predominantly in adult and fetal brain whereas the smaller transcript of approximately 10.3 kb is more widely expressed. The genetic defect leading to Huntington's disease may not necessarily eliminate transcription, but may confer a new property on the mRNA or alter the function of the protein. One candidate is the huntingtin-associated protein-1, highly expressed in brain, which has increased affinity for huntingtin protein with expanded polyglutamine repeats. This gene contains an upstream open reading frame in the 5' UTR that inhibits expression of the huntingtin gene product through translational repression. [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 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 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]
Huntingtin is a disease gene linked to Huntington's disease, a neurodegenerative disorder characterized by loss of striatal neurons. This is thought to be caused by an expanded, unstable trinucleotide repeat in the huntingtin gene, which translates as a polyglutamine repeat in the protein product. A fairly broad range in the number of trinucleotide repeats has been identified in normal controls, and repeat numbers in excess of 40 have been described as pathological. The huntingtin locus is large, spanning 180 kb and consisting of 67 exons. The huntingtin gene is widely expressed and is required for normal development. It is expressed as 2 alternatively polyadenylated forms displaying different relative abundance in various fetal and adult tissues. The larger transcript is approximately 13.7 kb and is expressed predominantly in adult and fetal brain whereas the smaller transcript of approximately 10.3 kb is more widely expressed. The genetic defect leading to Huntington's disease may not necessarily eliminate transcription, but may confer a new property on the mRNA or alter the function of the protein. One candidate is the huntingtin-associated protein-1, highly expressed in brain, which has increased affinity for huntingtin protein with expanded polyglutamine repeats. This gene contains an upstream open reading frame in the 5' UTR that inhibits expression of the huntingtin gene product through translational repression. [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 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 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]
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