The 3D structure of proteins Can often tolerate many individual amino acid subst
ID: 170377 • Letter: T
Question
The 3D structure of proteins Can often tolerate many individual amino acid substitutions. Is often only marginally stable under native conditions Sometimes shows conservation between distantly related proteins that is not obvious in sequence comparison All of the above None of the above in an aqueous solution, protein conformation is determined by two major factors. One is the maintenance of the maximum number of hydrogen bonds. The other is the: formation of the maximum number of hydrophilic interactions. maximization of ionic interactions. minimization of entropy by the formation of a water solvent shell around the protein. placement of hydrophobic amino acid residues within the interior of the protein. placement of polar amino acid residues around the exterior of the protein. Which of the following statements is false? Collagen is a protein in which the polypeptides are mainly in the alpha-helix conformation. Disulfide linkages are important for keratin structure. Glee residues are particularly abundant in collagen. Silk fibroin is a protein in which the polypeptide is almost entirely in the beta conformation. keratin is a protein in which the polypeptides are mainly in the a-helix conformation.Explanation / Answer
1. The native state or native conformation of a protein is its most typical conformation in a cellular environment. The native state is folded in a defined structure and the denatured state has random structure. The correct answer is option b.
2. In an aqueous solution, protein conformation is determined by two major factors. One is the formation of the maximum number of hydrogen bonds and the other is placement of hydrophobic amino acid residues within the interior of protein. The correct answer is option D.
3. Collagen is a protein in which the polypeptides are mainly in alpha-helix conformation is incorrect. Collagen actually forms right handed triple helix. So, statement a is incorrect.
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