7.1 Study Guide Flashcards
State which functional groups are shared by all amino acids. Explain the name ‘amino acid’ based on this information.
All amino acids share the quality of partially consisting of at least one amino group and one negative carboxyl group. This explains the name ‘amino acid’, as they all include an ‘amino’ group and carboxylic ‘acid’ due to their carboxyl group.
Explain the differences in complexity between each of the four levels of protein structure.
Primary Structure: Simply a chain of different amino acids covalently bonded together.
Secondary Structure: Folding of this chain into coiled and/or plated structures due to hydrogen bonding between the chained acids.
Tertiary Structure: Additional folding of the chain based on the water-related properties of each of its individual acids. These properties are determined by the acids’ side chains/R-groups, and this folding forms a functional protein.
Quaternary Structure: The binding of multiple tertiary structures, or polypeptides, together to produce a larger and more complex protein with a different function.
Describe what happens during and as a result of protein denaturation and give an example of a possible cause of it.
Protein denaturation is the process by which the bonds keeping a protein folded together, which give it its function, are broken by some force or energy, unraveling the protein and making it unfunctional. An example of a catalyst for this process would be extreme heat providing enough raw energy to destroy the bonds of the protein’s quaternary, tertiary, and even secondary structures.
Describe how the different groups of amino acids each affect tertiary structures of proteins in water.
Hydrophobic Acids: Due to their natural aversion to and inability to mix with water, hydrophobic amino acids turn and fold their sections of proteins inward to cover or ‘hide’ themselves from the water around them.
Hydrophilic Acids: Due to their natural attraction to and ability to mix with water, hydrophilic amino acids turn and fold their sections of proteins outward toward the water around them.
Acidic and Basic Acids: Due to having strongly opposite charges, acidic and basic amino acids naturally attract each other, pulling and twisting their proteins in whichever way moves them closer to each other so that they can form ionic bonds.
Cysteine Acids: Cysteine amino acids naturally bond with themselves due to being one of the few amino acids with sulfur, and they pull and twist their proteins in whichever way moves them closer to each other so that they can form bonds known as disulfide bridges.
True or False: Channel, Pump, and Receptor proteins work to build and break apart molecules for the body to use.
False. Channel, Pump, and Receptor proteins work to transport molecules, atoms, and nutrients around the body and around cell membranes; Enzymes are the proteins responsible for the building and breaking of molecules.
Explain why the body is able to produce antibodies specifically tailored to any intruding pathogen.
Because antibodies’ grappling arms use specific protein sets that allow them to take hold of specific pathogens, proteins’ practically limitless potential variability in amino acid sequence and, thus function, allows antibodies to be made to grab onto any specific pathogen that the body identifies.
Explain why collagen is one of the most important and numerous proteins in the body.
Collagen is so numerous and vital to the human body because it acts as a basic structure and structural support for an incredibly numerous amount of important body parts including bones, skin, teeth, and more.
Explain how and why the tertiary structure of a protein would shift as both a direct and indirect result of a hydrophilic amino acid being replaced with a hydrophobic one.
A direct result of a hydrophilic acid in a protein being replaced with a hydrophobic one would be an immediate inversion in the way that that acid’s section of the structure folds. Because hydrophilic and hydrophobic acids naturally move in opposite directions to each other from water, the section of the structure with the replaced acid would go from folding outwards toward water to folding inward away from water.
An indirect result of the acid replacement would stem from this change in folding. The changing of the protein’s structure in one location could very likely mess up the natural foldings caused by the other acids in the chain, leading them to fold the protein in even more new ways to re-satisfy their attractions or aversions.
How do the consequences of protein denaturation differ from those of protein mutation? In what ways are their consequences similar?
While protein denaturation and protein mutation both lead to the dysfunction of the protein at hand, they do so in different manners. Protein mutation alters the amino acid sequence in a protein, changing its natural shape and function and leaving it unable to perform the job it was originally meant to. Protein denaturation, however, completely unravels protein structures by breaking the bonds keeping them folded, which not only leaves them unable to perform their roles in the body but also leaves them completely unable to do anything at all.
