On the basis of the information provided in Figure 9.17, complete the mechanisms for peptide-bond cleavage by (a) a cysteine protease, (b) an aspartyl protease, and (c) a metalloprotease. 1bp...


On the basis of the information provided in Figure 9.17, complete the mechanisms for peptide-bond cleavage by (a) a cysteine protease, (b) an aspartyl protease, and (c) a metalloprotease.


A. Observed genetic variation<br>Substitution<br>>1bp indel<br>1bp indel<br>B. Mutation rate variation<br>FIGURE 9.17 The rate of mutation surrounding nucleosomes<br>is not constant. Substitution mutations peak in the nucleosomes<br>themselves, and are at a low point in the linker regions. Conversely,<br>insertion and deletion mutations (indel in the figure) are the opposite.<br>Researchers are attempting to establish why this is. (From Semple, C. A,<br>and Taylor, M. S. (2009). Molecular biology: The structure of change.<br>Science 323, 347-348. Reprinted with permission from AAAS.)<br>Frequency<br>

Extracted text: A. Observed genetic variation Substitution >1bp indel 1bp indel B. Mutation rate variation FIGURE 9.17 The rate of mutation surrounding nucleosomes is not constant. Substitution mutations peak in the nucleosomes themselves, and are at a low point in the linker regions. Conversely, insertion and deletion mutations (indel in the figure) are the opposite. Researchers are attempting to establish why this is. (From Semple, C. A, and Taylor, M. S. (2009). Molecular biology: The structure of change. Science 323, 347-348. Reprinted with permission from AAAS.) Frequency

Jun 11, 2022
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