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Most proteins have more leucine than histidine residues, but more histidine than tryptophan residues. Correlate the number of codons for these three amino acids with this information.

Short Answer

Expert verified
Explain the correlation. Answer: Yes, the number of codons for leucine, histidine, and tryptophan residues correlates with their occurrence in proteins. This is due to the fact that the higher the number of codons for an amino acid in the genetic code, the more likely it is to be present in proteins at a higher frequency. In this case, leucine has 6 codons, histidine has 2 codons, and tryptophan has 1 codon, resulting in the order of frequency: Leucine > Histidine > Tryptophan.

Step by step solution

01

Identify the codons for each amino acid

Refer to the codon table and identify the codons for leucine, histidine, and tryptophan. The codons for leucine are: UUA, UUG, CUU, CUC, CUA, and CUG. The codons for histidine are: CAU and CAC, and for tryptophan, only UGG.
02

Count the number of codons for each amino acid

Count the codons for each amino acid identified in Step 1:\[Leucine: 6\]\[Histidine: 2\]\[Tryptophan: 1\]
03

Correlate the number of codons to the occurrence of residues

It's stated that most proteins have more leucine than histidine residues and more histidine than tryptophan residues. The number of codons for each amino acid gives an indication of the probability of encountering that amino acid, since more codons increase the chances of encoding a particular amino acid during translation. Comparing the number of codons from Step 2, we see that the order of frequency for these amino acids correlates with the number of their respective codons:\[Leucine (6) > Histidine (2) > Tryptophan (1)\] This confirms that the number of codons for each amino acid correlates with the occurrence of these residues in most proteins. The higher the number of codons for an amino acid in the genetic code, the more likely it is to be present in proteins at a higher frequency.

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Most popular questions from this chapter

It has been suggested that the present-day triplet genetic code evolved from a doublet code when there were fewer amino acids available for primitive protein synthesis. (a) Can you find any support for the doublet code notion in the existing coding dictionary? (b) The amino acids Ala, Val, Gly, Asp, and Glu are all early members of biosynthetic pathways (Taylor and Coates, 1989 ) and are more evolutionarily conserved than other amino acids (Brooks and Fresco, 2003 ). They therefore probably represent "early" amino acids. Of what significance is this information in terms of the evolution of the genetic code? Also, which base, of the first two, would likely have been the more significant in originally specifying these amino acids? (c) As determined by comparisons of ancient and recently evolved proteins, cysteine, tyrosine, and phenylalanine appear to be late-arriving amino acids. In addition, they are considered to have been absent in the abiotic earth (Miller, 1987 ). All three of these amino acids have only two codons each, while many others, earlier in origin, have more. Is this mere coincidence, or might there be some underlying explanation?

What was the initial evidence for the existence of mRNA?

Recent observations indicate that alternative splicing is a common way for eukaryotes to expand their repertoire of gene functions. Studies indicate that approximately 50 percent of human genes exhibit alternative splicing and approximately 15 percent of disease-causing mutations involve aberrant alternative splicing. Different tissues show remarkably different frequencies of alternative splicing, with the brain accounting for approximately 18 percent of such events (Xu et al., 2002 . Nuc. Acids Res. \(30: 3754-3766\) ). (a) Define alternative splicing and speculate on the evolutionary strategy alternative splicing offers to organisms. (b) Why might some tissues engage in more alternative splicing than others?

When the amino acid sequences of insulin isolated from different organisms were determined, differences were noted. For example, alanine was substituted for threonine, serine for glycine, and valine for isoleucine at corresponding positions in the protein. List the single-base changes that could occur in codons of the genetic code to produce these amino acid changes.

An early proposal by George Gamow in 1954 regarding the genetic code considered the possibility that DNA served directly as the template for polypeptide synthesis. In eukaryotes, what difficulties would such a system pose? What observations and theoretical considerations argue against such a proposal?

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