Biology

Biology, 29.07.2019 12:30, Jael2

How does each snp affect the amino acid sequence of the insulin protein?

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Biology, 26.06.2019 04:00, dsporski

Need so bad. plz me! 1. if the dna sequence tca had a one base substitution to make it taa, which statement best describes how it would affect the protein? a.even though one letter changed, the same amino acid would still come in, so the protein wouldn't be altered. b.even though one letter changed, and one amino acid changed, the color of the amino acid stayed the same. therefore the protein's shape would not be altered. c.one letter changed and now instead of it being a white hydrophilic amino acid it is a yellow hydrophobic amino acid. this would cause the folding of the protein to alter as the yellow amino acid would force its way to the center of the protein. d.one letter changed and that would alter the entire reading frame of the protein and it would be so messed up a protein wouldn't even form.

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Biology, 31.07.2019 15:30, Kikilcaro9675

Human insulin has 50 amino acid in its protein sequence. the segment of dna that codes for the 51 amino acids in insulin has..a) 17 nucleotidesb) 50 nucleotidesc)100 nucleotidesd)150 nucleotides

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Biology, 13.09.2019 00:10, alyssamonae

The amino acid sequence of part of a protein has been determined: n…gly ala pro arg lys…c a mutation has been induced in the gene encoding this protein using the mutagen proflavin. the resulting mutant protein can be purified and its amino acid sequence determined. the amino acid sequence of the mutant protein is exactly the same as the amino acid sequence of the wild-type protein from the n terminus of the protein to the glycine in the preceding sequence. starting with this glycine, the sequence of amino acids is changed to the following: n gly his gin gly using the amino acid sequences, one can determine the sequence of 14 nucleotides from the wild-type gene encoding this protein. what is this sequence?

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Biology, 09.10.2019 23:00, shouyuanroh8462

Protein disulfide isomerase (pdi) is a protein folding enzyme that catalyzes disulfide–sulfhydryl exchange reactions. ribonuclease is an enzyme with two β-sheets, three α-helices, and four disulfide bridges critical to the stability of its structure. pdi rapidly converts inactive, scrambled ribonuclease to enzymatically active ribonuclease. this process is driven by the decrease in free energy as the scrambled conformations are converted into the stable, active conformation of the enzyme. in contrast, pdi rapidly inactivates insulin. what does pdi's effect on insulin imply about the structure of insulin? the three‑dimensional shape of insulin does not contain any disulfide bonds. the active conformation of insulin has more β-sheets than α-helices. the amino acid sequence of insulin is similar to the amino acid sequence of ribonuclease. the active conformation of insulin is not the most thermodynamically preferred form.

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