the hydrogen bonds would be lost, affecting a hell and pleated sheet formation C.the protein would lose peptide bond formation, and thus it would lose Its primary structure. the structure of the protein would not change, because both residues have hydrophobic properties. the protein would lose activity, but the structure would remain the same. the hydrogen bonds would be lost, affecting a helix and pleated sheet formation O B. the protein would lose disulfide bond formation, which would affect the stability of its tertiary structure. the protein would lose peptide bond formation, and thus it would lose its primary structure. the structure of the protein would not change, because both residues have hydrophobic properties B.the protein would lose activity, but the structure would remain the same. If all of the cysteine amino acids of a protein were changed to threonines, which statement best describes what would happen? A. Humans and chimpanzees are so closely related that all of their protein sequences are identical. The two proteins will have the same properties, since they have the same primary structure, but different functions, since they come from different species. The folding is likely to difter in the polypeptide chains in the two cases because they endst In cels of different organisms. Which statement related to this observation is most accurate? The two proteins serve the same function in both humans and chimpanzees because their structures are the same The biological properties of the two proteins must differ, since they were isolated from two different species. The amino acid sequence of a protein isolated from human blood cells is the same as the amino acid sequence of a protein isolated from chimpanzees. Ophe and Asp are hydrophilic and likely could interact with targeted proteins because they could stick out from the Insulin polypeptide backbone. There are major differences in the amino acids at A3 and 12 that could likely affect the guinea pig Insulins ability to interact with target proteins in peanut. The guinea pig and dog amino acid sequence are the same so this is a fine treatment for peanut. O Phe and Gly are hydrophobic and likely could interact with targeted proteins because they could stick out from the Insulin polypeptide backbone. Which statement is the most accurate? Species A1 A2 A3 A4 A5 A19 A21 B12 B16 B23 B24 325 326 Canine Glylle Val Glu Gin Tyr Asn Val Tyr Gly Phe Phe Tyr Guinea pig Phe Asp - Gly Wood fros Ser - Surinam toad - His - Cod Asp Eel - 1 Phe Tilapia Glu - O Phe and Gly are hydrophilic and lively could interact with targeted proteins because they could stick out from the Insulin polypeptide backbone. The following data is hypothetical but let's say the veterinarian proscribed guinea pig insulin to a tiny dog named peanut. Sometimes veterinarians prescribe injections of pig insulin to dogs for treatment. O hydrogen bonding of the N-H groups on one amino acid and the CD groups on another. O peptide bond formation between cysteines that are regularly spaced along peptide chains. O the N-C-Crepeat of the peptide backbone, allowing for regularly spaced peptide bonds between chain segments. O the hydrophobic nature of the chains, which causes the chain to coll with the groups inward. In an alpha helix the coiling is stabilized by Time Run Attempted 1 Hour, 4 O repulsion of the chains from each other, causing the coll to form with the groups on the outside.
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