When comparing primary sequence of a protein between species, it is often noted that glycines and...
Homework Answers
Glycines and cysteines are highly conserved.This is because :
- Glycine has the smallest side chain and this side chain allows most polypeptides to make tight turns and also helps them to approach each other closely.
- Cysteine possesses sulfudryl groups that makes disulfide bridges.These disulfide bridges plays a major role in the stabilization of protein structure at higher levels and replacing them would have dramatic effect on the overall structure of entire protein.
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When comparing primary sequence of a protein between species,
it is often noted that glycines and...
1.When comparing similarities among multiple protein structures, which of the following is false? (Level of Difficulty:...
1.When comparing similarities among multiple protein structures, which of the following is false? (Level of Difficulty: Difficult) A) Proteins with the same function from a different species are likely to have similar motifs. B) Proteins with the same function from different species are likely to be more similar in sequence than in structure. C) An effective protein motif is likely be observed in multiple proteins. D) Proteins with the same motifs are likely to perform similar functions. E) None of...
In comparing species using a protein cladogram and a DNA cladogram, how do you know which...
In comparing species using a protein cladogram and a DNA cladogram, how do you know which cladogram is correct or the most accurate? Do you think one of the cladograms is better or more reliable than the other? Why?
Sequence Comparisons Proteins called molecular chaperones (described in Chapter 4) assist in the process of protein...
Sequence Comparisons Proteins called molecular chaperones (described in Chapter 4) assist in the process of protein folding. One class of chaperone found in organisms from bacteria to mammals is heat shock protein 90 (Hsp90). All Hsp90 chaperones contain a 10 amino acid "signature sequence," which allows for ready identification of these proteins in sequence databases. Two representations of this signature sequence are shown below. (a) In this sequence, which amino acid residues are invariant (conserved across all species)? (b) At...
A geneticist has studied the sequence of a gene in each of three species, A, B,...
A geneticist has studied the sequence of a gene in each of three species, A, B, and C. Species A and species B are sister species; species C is more distantly related. The geneticist has calculated the ratio of nonsynonymous (NS) to synonymous (S) nucleotide substitutions in the coding region of the gene in two ways—first, by comparing the gene sequences of species A and C, and second, by comparing the gene sequences of species B and C. The NS:S...
Consider an important protein like beta-galactosidase, which breaks down lactose. Many bacterial species have beta-galactosidase. But...
Consider an important protein like beta-galactosidase, which breaks down lactose. Many bacterial species have beta-galactosidase. But that doesn't mean that the amino acid sequence of beta- galactosidase in all those bacterial species is exactly the same. Far from it. As bacteria diversified into different species over evolutionary time, beta-galactosidase encoded in the genomes of the bacteria also diversified. However, we can assume that even though beta-galactosidase diversified, it was under pressure to maintain structure and function, because the reaction it...
A part of the aminoacid sequence in Cytochrome-C protein from 6 different species is given in...
A part of the aminoacid sequence in Cytochrome-C protein from 6 different species is given in the table. Rank the organisms from 1 to 5 according to the similarity of the organism to human: based on the similarity between the cytochrome C aminoacid sequences, 1 being the closest to human. It is largely agreed that the greater the number of amino acid (or nucleotide) differences between a given pair of organisms, the further apart they are in evolution. On the...
what are the key differences between protein domains and sequence features?
what are the key differences between protein domains and sequence features?
If one wishes to examine a chemical species dissolved in aqueous solution, it is often much...
If one wishes to examine a chemical species dissolved in aqueous solution, it is often much better to use Raman spectroscopy instead of IR spectroscopy.Predict why this might be true.
If you have an enzyme that has a primary sequence that is 429 amino acids in...
If you have an enzyme that has a primary sequence that is 429 amino acids in length, is it possible that both an amino acid position 215, as well as amino acids located at 342, and 401, can all be part of an active site of a protein? Explain why or why not?
3. You modify GDP (green fluorescent protein) to contain a signal sequence you believe is a...
3. You modify GDP (green fluorescent protein) to contain a signal sequence you believe is a novel ER import signal at the N-terminus and a stop transfer sequence 43 amino acids from the N terminal import signal. When this protein is expressed in cells, you see 70% GFP in the cytoplasm and the remainder in the ER. You assume GFP import is occurring. However you cannot rule out some GFP might not fold properly even though it is fluorescent, perhaps...
Sequence Comparisons Proteins called molecular chaperones (described in Chapter 4) assist in the process of protein folding. One class of chaperone found in organisms from bacteria to mammals is heat shock protein 90 (Hsp90). All Hsp90 chaperones contain a 10 amino acid "signature sequence," which allows for ready identification of these proteins in sequence databases. Two representations of this signature sequence are shown below. (a) In this sequence, which amino acid residues are invariant (conserved across all species)? (b) At...
Consider an important protein like beta-galactosidase, which breaks down lactose. Many bacterial species have beta-galactosidase. But that doesn't mean that the amino acid sequence of beta- galactosidase in all those bacterial species is exactly the same. Far from it. As bacteria diversified into different species over evolutionary time, beta-galactosidase encoded in the genomes of the bacteria also diversified. However, we can assume that even though beta-galactosidase diversified, it was under pressure to maintain structure and function, because the reaction it...
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