cellular and molecular biology
Answer the following Discussion Forum question(s): How can 20 different amino acids create all of the thousands of different proteins we have? How do proteins achieve four levels of structure? Do all proteins have all four levels? What is denaturation? Give an everyday example of how humans use protein denaturing to our advantage. Make sure your answer is different from other students!!! Response is at least 250 words long, answers questions clearly and correctly, includes examples/ideas that are different from other student . CiItation for sources provided using proper APA citation. other students answer is 1- It is possible for the 20 amino acids to create the thousands of different structures of protein we have simply because there are thousands of sequences they can be arranged in! The order in which the amino acids are sequenced codes for a specific protein and its distinct characteristics. The smallest change in a sequence can entirely change a protein’s biological function. In addition, these amino acid sequences also demonstrate a great variation in length of polypeptides–they could have a very short chain length or thousands of amino acids long. Changes in the amino acid sequence can also change a protein’s structure. Most proteins achieve their desired structure via interactions between certain groups of amino acids. Not all proteins have all four structure levels in their synthesis process, but most have the primary, secondary, and tertiary structures. The quaternary structure is made up of multiple polypeptide chains, making it the most complex structure (Khan Academy, 2015).
Denaturation describes the process of breaking weak bonds within a protein that alters its structure and biological function; these proteins generally become non-functional (Khan Academy, 2015). The proteins will simply be reduced to their primary structure. Denaturation can be caused by many factors, some of which are changes in temperature and pH that put proteins outside of their optimal conditions, therefore limiting their effectiveness and function. Humans often denature proteins to our advantage, and one common example is cooking eggs or raw meat, making them safer to eat and easier to digest. Cooking these food items also kills potential pathogens that are harmful to our digestive system, like salmonella.
Citations:
Khan Academy. (2015). Orders of Protein Structure. Khan Academy. https://www.khanacademy.org/science/biology/macromolecules/proteins-and-amino-acids/a/orders-of-protein-structure.
2- Twenty different amino acids create thousands of different proteins through the vast array of possible sequences and combinations. Each amino acid sequence, determined by the order of nucleotides in DNA, forms a unique polypeptide chain. These chains fold into specific shapes, achieving four levels of structure that determine the protein’s function.
The primary structure is the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from hydrogen bonds between the backbone atoms in the polypeptide chain, forming ?-helices and ?-pleated sheets. The tertiary structure results from interactions between the side chains (R groups) of the amino acids, including hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges, giving the protein a three-dimensional shape. The quaternary structure occurs when two or more polypeptide chains (subunits) join to form a functional protein complex.
Not all proteins have all four levels of structure. Some proteins, like myoglobin, consist of a single polypeptide chain and only achieve tertiary structure. In contrast, proteins like hemoglobin, which have multiple polypeptide subunits, exhibit quaternary structure.
Denaturation is the process by which a protein loses its native shape due to the disruption of weak chemical bonds and interactions, often caused by changes in pH, temperature, or exposure to chemicals. This loss of structure results in the loss of function. An everyday example of protein denaturation is cooking an egg. The heat from cooking breaks the weak interactions in the egg white proteins, causing them to unfold and coagulate into a solid, white mass. This denaturation process makes the proteins more digestible, demonstrating how humans use protein denaturation to our advantage by making nutrients more accessible.
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