Etched & Amino acid
Compare and contrast the variety of amino acids with that of monosaccharides and fatty acids. Which group exhibits the greatest structural variability? A: There are twenty amino acids, with that there are only three types of monosaccharides; the large variety is because of the constant change in the R groups. The three monosaccharides are fructose, galactose and glucose. In comparison, there are only two types of fatty acids, those being, unsaturated and saturated. The group that exhibits the greatest structural variability is amino acids .
How does the molecular structure of urea suit its biological function? A: The urea contains two nitrogen atoms for every carbon atom; it is soluble very in water, this provides the body with a device that can easily remove access nitrogen (waste). Q: Describe the appearance and arrangement of amino acids in a-helix and b-pleated sheet regions of polypeptides. What type of intermolecular forces are involved in maintaining protein secondary structure? A: Amino acids are linked together in such an arrangement that they form long polypeptide chains.
The alpha helix is formed when the polypeptide chains twist in a spiral manner. This enables all of the amino acids in the chain to form hydrogen bonds with each other. An example of an alpha helix assembly is fingernails. The beta-pleated sheet is polypeptide chain running along side each other; this gives the arrangement a wave-like illusion. Beta-pleated sheets are also linked together by hydrogen bonds.
An example of beta-pleated sheets is a feather. Q: Describe and give examples of proteins that have a variety of tertiary structures. Relate the tertiary structure of these proteins to their biological functions. A: Myoglobin has compressed globular tertiary structure that makes it suitable for transporting oxygen. Silk is very strong because it is composed of many parallel chains of beta-pleated sheets. Collagen is made up of a noticeably different secondary structure known as a triple helix that creates an extremely strong, linear structure.
What special role is played by the amino acid cysteine? How do disulphide bridges influence protein shape and stability? A: The special role that is played by the amino acid cysteine is that it is able to form disulphide bridges. Disulphide bridges influence protein shape and stability by preventing the polypeptide from changing shape under regular conditions. High temperatures and/or chemical action can cause the polypeptide to alter its natural qualities. Q: Do all proteins
have quaternary structure? Support your answer with examples.
No, not all proteins have quaternary structures. Quaternary structures are only for proteins that contain multiple subunits. For example, Hemoglobin has four subunits, which renders it a quaternary structure.
Q: Describe the structure of ATP. What is the primary function of ATP within living organisms? A: ATP is made up of a nitrogenous base (adenine), a simple sugar (ribose) and 3 phosphate groups. ATP has a variety of functions in living organisms, mostly involving energy transfer during the metabolic process but ATP also helps move substances across cell membranes, supplies the energy needed for muscles to contract, it carries the energy needed to synthesize the many types of macromolecules that the cell.
What bases are building blocks of nucleotides within RNA and DNA, respectively? A: The bases that are the building blocks of nucleotides within RNA are Adenine, Guanine, Cytosine, and Uracil. The bases that are then building blocks of nucleotides within DNA are Adenine, Guanine, Cytosine, and Thymine Q: List some of the structural similarities and differences between transfer RNA and DNA. A:
Ribose sugar present
Two double chains held in a double helix by hydrogen bonds
Sugar linked to a phosphate group at one end and a nitrogenous base at the other Polymer of nucleotides
Q: How are the bases paired within the DNA double helix? What type of bonding is responsible for the forces maintaining these base pairings and the double helix? A: The bases are paired Adenine and Thymine & Guanine and Cytosine held together by hydrogen bonds. 2 for A-T and 3 for G-C.