midterm_2_answers

midterm_2_answers - 1. In an aqueous solution, protein...

Info iconThis preview shows pages 1–3. Sign up to view the full content.

View Full Document Right Arrow Icon
1. In an aqueous solution, protein conformation is determined by two major factors.One is the formation of the maximum number of hydrogen bonds.What is the other more important factor? A) formation of the maximum number of hydrophilic interactions. B) maximization of ionic interactions. C) minimization of entropy by the formation of a water solvent shell around the protein. D) placement of hydrophobic amino acid residues within the interior of the protein. E) placement of polar amino acid residues around the exterior of the protein. 2. Choose the one true or false statement? A) Collagen is a protein in which the polypeptides are mainly in the -helix conformation. False B) Disulfide linkages are important for keratin structure. C) Gly residues are particularly abundant in collagen. D) Silk fibroin is a protein in which the polypeptide is almost entirely in the conformation. E) -keratin is a protein in which the polypeptides are mainly in the -helix conformation. 3. Determining the precise arrangement of atoms within a large protein is possible only through the use of: A) electron microscopy. B) light microscopy. C) molecular model building. D) Ramachandran plots. E) x-ray diffraction. 4. Which of the following best fills in this blank? The subunit interface in a multisubunit protein largely consists of ______ amino acid side chains. A) Positively charged B) Nonpolar C) Polar D) Negatively charged
Background image of page 1

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
A) They are a form of secondary structure. B) They are examples of structural motifs. C) They may retain their correct shape even when separated from the rest of the protein. D) They have been found only in prokaryotic proteins. E) They consist of separate polypeptide chains (subunits). 6. How does the native structure of a protein differ from the denatured state? A) the native structure is higher in energy than the denatured form B) the native state always has disulfide bonds and the denatured state does not. C) the native structure is formed from the denatured state by the addition of urea to the denatured state. D) the native state is folded in a defined structure and the denatured state has random structure E) denatured proteins have a much higher percentage of polar amino acids than the native structure. 7. Choose the one true or false statement regarding oligomeric proteins? A) A subunit may be similar to other proteins. B) All subunits must be identical. False C) Many have regulatory roles. D) Some oligomeric proteins can further associate into large fibers. E) Some subunits may have nonprotein cofactors. 8. Protein S will fold into its native conformation only when protein Q is also present in the solution.However, protein Q can fold into its native conformation without protein S.Protein Q, therefore, may function as a ____________ for protein S. A)
Background image of page 2
Image of page 3
This is the end of the preview. Sign up to access the rest of the document.

Page1 / 10

midterm_2_answers - 1. In an aqueous solution, protein...

This preview shows document pages 1 - 3. Sign up to view the full document.

View Full Document Right Arrow Icon
Ask a homework question - tutors are online