
Biology (MindTap Course List)
11th Edition
ISBN: 9781337392938
Author: Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg
Publisher: Cengage Learning
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Transcribed Image Text:Which of the following is incorrect about the beta-sheet?
a. The strands in anti-parallel beta-sheets are usually connected with turns
b. Side chains are alternated above and below the sheet
C. Parallel beta-sheets are less stable than the anti-parallel ones
Od. It is stabilized by hydrophobic interactions between the side chains of nonpolar residues
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- Pyrimidines built from a single carbon ring are: a. cytosine and thymine. b. adenine, cytosine, and guanine. c. adenine and thymine. d. cytosine and guanine. e. adenine and guanine.arrow_forwardPathogenic E. coil have recently been shown to degrade tight junction proteins during infection. How would this provide an advantage to the bacteria?arrow_forwardUsing Figures 8.7 and 8.9 as a guide, draw a dinucleotide composed of C and A. Next to this, draw the complementary dinucleotide in an antiparallel fashion. Connect the dinucleotides with the appropriate hydrogen bonds. FIGURE 8.9 The two polynucleotide chains in DNA run in opposite directions. The left strand runs 5 to 3, and the right strand runs 3 to 5. The base sequences in each strand are complementary. An A in one strand pairs with a T in the other strand, and a C in one strand is paired with a G in the opposite strand. FIGURE 8.7 Nucleotides can be joined together to form chains caled polynucleotides. Polynucleotides are polar molecules with a 5 end (at the phosphate group) and a 3 end (at the sugar group). An RNA polynucleotide is shown at the left, and a DNA polynucleotide is shown at the right.arrow_forward
- Describe the four levels of protein structure. How do a proteins side groups influence its interactions with other substances? What happens when a protein is denatured?arrow_forwardAmino acids have the generic structure seen below, where R represents different carbon-based side chains. Describe how the structure of amino acids allows them to be linked into long peptide chains to form proteins.arrow_forwardUnderstanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules, can be characterized in terms of general properties such as size, shape, charge, solubility/hydrophobicity. Consider the influence of each of these general features on the likelihood of whether folding of a particular protein will require chaperone assistance or not. Be specific regarding just Hsp7O chaperones or Hsp7O chaperones and Hsp60 chaperonins.arrow_forward
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