What could Carl Linnaeus no have used as a method of classification in his taxonomy system ?

5. Circle the three anti-codons at the

mixas84 [53]

Answer:

5. Circled in red on attachment

6. Green arrows on attachment

7. Orange box in the attachment

8. Circled red on attachment

9. Blue boxes on attachment

10. Black line on attachment

11. It has already disassociated

12. Purple rectangle in attachment

13. GAC

14. Leucine

Explanation:

I think most of this worksheet is to be completed on your own model of transcription that you have made, however, I will label the diagram

5. tRNA molecules bring amino acids to the ribosome. They are recognisable by their "cloverleaf" shape. In the picture, you can see that they are attached to amino acids (and you can even see some in the ribosome). The codons are on the opposite side of the tRNA to the amino acid, and are 3 bases complementary to the codon on the mRNA, represented here as 3 rectangles.

6. As described above, you can see some tRNAs in the ribosome. These tRNAs have paired up with complementary codons on the mRNA strand via their anti-codons. This is indicated by the green arrow. This is how the mRNA dictates the sequence of the polypeptide chain and makes protein

7. I think this question is just checking you know where the amino acid goes. The amino acid is attached to the opposite site of the anti-codon indicated in the image.

8. The anticodon in the tRNA has been indicated in question 5. Anticodons refer to three bases that are complementary to a specific codon on mRNA, and specify a particular amino acid

9. Each codon refers to each triplet of nucleotides in the mRNA. I have indicated this as blue boxes on the mRNA transcript. You can tell where they are based on where the tRNA is binding, always in 3s

10. See the black line, this is a called a peptide bond, and is the bond that joins together the amino acids in a growing polypeptide chain. I have drawn it between the first two amino acids in the second image. The amino acids represent a string of molecules linked using this peptide bond, which is a covalent bond formed by a condensation reaction

11. The first tRNA is not shown in the second diagram because the peptide bond has already formed between Valine and Histidine, so the tRNA that brought Valine to the machinery has disassociated from Valine and the ribosome. It is then free to bind another Valine and join in other translation processes

12. The third codon is CUG. We can see the first codon is GUG, then CAU, and the next is CUG. This is labelled with a purple rectangle in the attachment

13. Base pairing rules state that C pairs with G, and that A pairs with U (or T on DNA). The codon is CUG, therefore the anti-codon must be GAC

14. Each codon corresponds to a particular amino acid sequence. The codon CUG corresponds to the amino acid Leucine. You can find this using a codon table, like the one attached here

6 0

4 years ago

How did the Oregon system make the political process more democratic

N76 [4]

Answer:

generally considered to have originated in the late nineteenth century as a reaction to the abuses of big business and the problems that plagued the lower socio-economic classes of that era.

Explanation:

3 0

4 years ago

What natural agent of erosion is mainly responsible for the formation of the barrier islands along the southern coast of Long Is

jolli1 [7]

The ocean since erosion gets minerials from one place to another the ocean is the reason of the formation since the ocean is the only thing that could form its because of the waves

8 0

4 years ago

Read 2 more answers

Use this space to map your dystrophin analogy. Make sure to include sarcolemma (cell membrane),

Anastaziya [24]

Abstract

The dystrophin complex stabilizes the plasma membrane of striated muscle cells. Loss of function mutations in the genes encoding dystrophin, or the associated proteins, triggers instability of the plasma membrane and myofiber loss. Mutations in dystrophin have been extensively cataloged providing remarkable structure-function correlation between predicted protein structure and clinical outcomes. These data have highlighted dystrophin regions necessary for in vivo function and fueled the design of viral vectors and now, exon skipping approaches for use in dystrophin restoration therapies. However, dystrophin restoration is likely more complex, owing to the role of the dystrophin complex as a broad cytoskeletal integrator. This review will focus on dystrophin restoration, with emphasis on the regions of dystrophin essential for interacting with its associated proteins and discuss the structural implications of these approaches.

Keywords: muscular dystrophy, dystrophin, spectrin repeat, exon skipping, sarcoglycan, sarcolemma

Go to:

INTRODUCTION

Muscular dystrophy is a collection of inherited diseases characterized by skeletal muscle weakness and degeneration. Muscular dystrophies are progressive disorders because over time healthy muscle fibers are lost and replaced by fibrosis and fat, making muscle tissues less able to generate force for everyday activity. As muscle wasting ensues, patients experience weakness, although muscle groups may be targeted differently in specific forms of muscular dystrophy. Respiratory failure, resulting from the weakening of breathing muscles, may limit lifespan in muscular dystrophy unless mechanical support is instituted. In some forms of muscular dystrophy, the heart is also affected resulting in cardiac complications including heart failure and irregular heart rhythms.

Duchenne muscular dystrophy (DMD) is one of the most common forms of muscular dystrophy. DMD is caused by recessive mutations in the dystrophin gene on X chromosome, affecting 1 in 3,500 to 5,000 newborn males worldwide (82). Boys with DMD show signs of muscle weakness early in childhood, typically between 2 and 7 years of age, and often lose ambulation around the time of puberty. DMD boys may have delayed development of motor skills such as sitting, walking and talking. Becker muscular dystrophy (BMD) is also caused by mutations in the DMD gene that encodes dystrophin. Individuals with BMD share similar signs and symptoms with DMD boys but with later onset and more varied time course. Like DMD, the heart can be affected in BMD.

The dystrophin gene is the largest known human gene, containing 79 exons and spanning > 2,200 kb, roughly 0.1% of the whole genome (96). The most common mutation responsible for DMD and BMD is a deletion spanning one or multiple exons. Such deletions account for 60–70% of all DMD cases and 80~85% BMD cases (58, 147). Point mutations are responsible for around 26% of DMD cases and 13% BMD cases. Exonic duplications account for 10 to 15% of all DMD cases and 5% to 10% BMD cases. Subexonic insertions, deletions, splice mutations and missense mutations account for the rest of the cases. DMD is associated with mutations that disrupt the protein’s reading frame causing premature stop codons. These mutated transcripts are susceptible to nonsense mediate decay, and the carboxy-terminal truncated protein products are also unstable and subject to degradation, leaving little or no protein produced in cells. In contrast, BMD patients usually have in-frame deletions that maintain the correct reading frame. Furthermore, nonsense mutations have been associated with both BMD and DMD. However, nonsense mutations associated with BMD are more prone to induce exon skipping than those found in DMD (59). The resulting protein products in BMD are internally truncated and expressed at lower levels than normal muscle. However, these internally truncated proteins are expressed at higher levels than in DMD and remain partially functional. Within one BMD affected family, three males carrying the same nonsense mutation in exon 29 displayed phenotypes from severe, mild to asymptomatic. This nonsense mutation is located in an exon recognition sequence in exon 29 and induces partial skipping of exon 29, producing an internally truncated dystrophin. A considerable amount s

7 0

2 years ago

Four types of functional groups?

julia-pushkina [17]

<span> carbonyl, carboxyl, phosphate, and methyl</span>

5 0

3 years ago