gen bio protein and nucleic acid

• Nucleic Acids such as nucleotides which contain atoms of carbon, hydrogen, oxygen, nitrogen, phosphorus
• Proteins such as amino acids which contain atoms of carbon, hydrogen, oxygen, nitrogen
• High levels of triglyceride in the body can block the blood vessels due to the formation of plaque that could trigger a cardiovascular problem.
• Proteins and nucleic acids are important biomolecules needed for different dynamic processes in living organisms.

  Different biological processes require the presence of proteins. Nucleic acids are biomolecules responsible for storing, transmitting, and expressing hereditary information. Life would not be possible without these two biomolecules.
• Proteins have many functions and are essential to our everyday activities.
• Proteins consist of long chains of amino acids called polypeptides.
• Amino acids are the monomers or building blocks of proteins.
• There are usually 100 to 10,000 amino acids in a typical protein molecule.
• Millions of combinations of amino acids are also possible.
• Amino acids have a central or alpha carbon, to which the following are bonded: an amino group, hydrogen, a carboxyl group, and a unique side chain, also known as the R-group.
• There are 20 common amino acids found in proteins.
• These molecules differ in their unique side chains.
• the functionality of a protein structure depends on the following four hierarchical organizations:

  primary, secondary, tertiary, and quaternary structures. The interactions that take place between the different protein structures give them three dimensional arrangements that enable them to facilitate different functions in the body.
• Primary structure is a linear chain of amino acids in a polypeptide strand.
• The amino acid sequence is the main determinant of the overall structure of the protein.
• The amino acid sequence also determines the amino acid chain's ultimate biological function.
• Secondary structure refers to the local three-dimensional folding of the polypeptide chain in the protein.
• The alpha helix (spiral) and the beta sheet (beta strand forming an accordion-like pleated sheet) are the two more common secondary structure motifs.
• Varying arrangements of weak hydrogen bonds are responsible for these configurations.
• Tertiary structure is formed when the distant segments of a primary structure and the relationships of the side chains are bound in a three-dimensional folding of the entire polypeptide chain.
• Tertiary structure is stabilized both by non-covalent (hydrophobic interactions, electrostatic bonds, hydrogen bonding, Van der Waals forces), and covalent (disulfide) bonds.
• Quaternary structure involves the fitting together of two or more polypeptide chains, eventually forming a functional protein.
• Quaternary structure is stabilized by the same bonds as those in the tertiary structure.
• An example of a protein with a quaternary structure is hemoglobin.
• Subunit or domain is the term used to denote each chain in a protein.
• Structural proteins are proteins involved in maintaining the shape and framework of the cell.
• Proteins that bind to segments of DNA and control the replication of DNA in mitosis and meiosis are known as chromosomal proteins.
• Collagen is the most abundant protein found in the human body.
• Transport proteins carry other substances in and out of cells.
• Collagen gives strength and support to tissues that undergo continual wear and tear such as skin and bone.
• Regulatory proteins control numerous cell processes.
• Collagen is a type of structural protein that is fibrous in nature.
• Transport proteins are involved in cell transport as discussed in Chapter 1.
• Enzymes facilitate many chemical reactions. They do this by lowering the amount of energy needed to start the reaction while not being permanently altered in the process. The induced fit model describes how enzymes work.

  There is an active site in the enzyme with which specific molecules, called substrates, interact.

  This interaction causes the enzyme to change shape, which favors a chemical reaction. Enzymes are affected by pH and temperature.
• Hormones serve as chemical messengers. They carry instructions from more than a dozen glands and tissues all over the body. They are carried by the blood or by the fluid around cells towards the target cells, where their effects are manifested. Only those cells with specific protein receptors can recognize them.
• Defense proteins such as antibodies are highly specific proteins that are responsible for detecting a foreign substance or "antigen." The body produces a specific antibody to respond to an antigen to inactivate it.
• A good example to see how antibodies work is to know how vaccines work in the body.
• Vaccination is the process of introducing an antigenic material that has been reduced to minimum amounts or has been attenuated (weakened in a susceptible host) for the purpose of increasing immunity to a particular infectious agent (e.g., bacteria and viruses).
• During the first immune response, the primary antibodies produced are of the IgM type, and this is followed by the IgG type a few days later.
• The adaptive immune response is able to eliminate the agent, causing some of the lymphocytes to become memory cells.