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14: Introducing LINQ
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10. Observing and Inferring Describe the appearance of the precipitate. What is the
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In this exercise, you will use the CLI to create a basic configuration. You ll perform these steps on the routers and switches using Boson s NetSim simulator. (You can find a picture of the network diagram for the simulator in the Introduction section of this book.) After starting up the simulator, do the following: 1. Click the LabNavigator button. At the top of the simulator in the menu bar, click the eRouters icon and choose 2600-1. 2. Starting with the 2600-1 router, go to Privilege EXEC mode and then enter Configuration mode: At the top of the simulator s toolbar, click the eRouters icon and select 2600-1. On the 2600-1 router, access User EXEC mode and use enable to go to Privilege EXEC mode, and then use configure terminal to access Configuration mode. 3. Assign a hostname of 2600-1: Use the hostname 2600-1 command and examine the prompt. 4. Set a User EXEC password of cisco for telnet access: Enter the line vty 0 4 command and follow it with the login and password cisco commands. Exit this subcommand mode: exit. 5. Assign an encrypted Privilege EXEC password of cisco: Enter enable secret cisco. 6. Check whether or not the serial 0 interface is DTE or DCE. If it is DCE, assign a clock rate of 64,000: Check the controller from Privilege EXEC mode using show controller serial 0. 7. If it s the DCE, configure the clock rate by performing the following. Enter the interface with configure terminal and interface serial 0. Configure the clock rate: clock rate 64000. 8. Enable the fastethernet0/0 interface: interface fastethernet0/0, no shutdown, and exit. 9. Enable the serial0 interface: interface serial0, no shutdown, and exit. Exit to Privilege EXEC mode: end.
favorable free-energy change for this sulfur atom to form a covalent bond with another sulfur atom on another cysteine residue. Such a covalent bond between two sulfur atoms, attaching two cysteine residues together, is called a disulfide bond. Many proteins contain cysteine residues some distance away from each other in the amino acid chain. Figure 9-3 shows the formation of a disulfide bond. Disulfide bonds contribute favorably to the free energy of protein folding. In addition, once formed they add some rigidity to a protein secondary and tertiary structure, enabling the structure to withstand a significant amount of bumping about and stress while still maintaining its native state. The formation of disulfide bonds is a type of cross-linking (Chap. 6) a covalent connecting of parts of a molecule that are distant in primary structure but come together (and cross-link) in the secondary or tertiary structure.
TABLE 6.1 ATM Conformance vs. Interoperability.
Chemistry: Matter and Change 20
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