By Sandro Carrara
The program of CMOS circuits and ASIC VLSI platforms to difficulties in medication and method biology has ended in the emergence of Bio/CMOS Interfaces and Co-Design as a thrilling and swiftly starting to be quarter of study. The mutual inter-relationships among VLSI-CMOS layout and the biophysics of molecules interfacing with silicon and/or onto metals has ended in the emergence of the interdisciplinary engineering method of Bio/CMOS interfaces. This new technique, facilitated by means of 3D circuit layout and nanotechnology, has led to new ideas and purposes for VLSI platforms within the bio-world.
This booklet deals a useful connection with the state of the art in Bio/CMOS interfaces. It describes modern study within the box of CMOS layout and VLSI improvement for functions requiring integration of organic molecules onto the chip. It presents multidisciplinary content material starting from biochemistry to CMOS layout as a way to tackle Bio/CMOS interface co-design in bio-sensing applications.
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Exercise 10 Does a polypeptide composed of arginine, alanine, isoleucine, lysine, methionine, threonine, and glycine possess a hydrophobic character? Exercise 11 What are the possible conformations of the polypeptides contained in an antibody? Exercise 12 Why is protein flexibility so important in proteins’ biological functions? Exercise 13 Why are adenine, guanine, cytosine, and thymine called bases? Exercise 14 What is the difference between a nucleic acid and aspartic acid? Exercise 15 List all the differences between DNA and RNA.
As we saw in the previous chapter, solution ions within a Debye length contribute to Helmholtz layers. We will see in this chapter that complex biological molecules, such as proteins or DNA, also carry electrical charges that are usually distributed along the molecule. These charges also generate electrical interactions with circuits. Therefore, all biological molecules present in the system we are S. 1007/978-1-4614-4690-3_3, # Springer Science+Business Media New York 2013 29 30 3 Biochemistry of Targets and Probes interfacing will have significant interaction with the surface of our circuits.
The channels’ subunits must be free to move in order to open and close the ion flow as required. Thus, the connections in the random coils are very important for providing structural flexibility. Flexibility plays the most important role in protein function. Some proteins’ active sites need flexibility to grasp target molecules. The active site of a protein is the molecular region that exploits the protein’s function. If a protein has as its function the transformation of a target molecule, then its active site has the correct tertiary structure and the correct flexibility for enabling the protein to block and transform the target.