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BioHnrs Unit 1 Study
This is to help me study for the Unit 1 Biochemistry test in Biology Honors.
| Term | Definition |
|---|---|
| Reactants | The starting substances in a chemical reaction. |
| Products | The substances formed as a result of a chemical reaction. |
| Organic Compounds | Compounds that always contain carbon and usually have hydrogen, oxygen, nitrogen, phosphorus, or sulfur. |
| Polymers | Large molecules made up of smaller repeating units called monomers. |
| Monomers | Individual subunits that make up polymers. |
| Anabolic Reaction | A chemical reaction that builds larger molecules from smaller ones and requires energy. |
| Catabolic Reaction | A chemical reaction that breaks down larger molecules into smaller ones and releases energy. |
| Dehydration Synthesis | A chemical process that builds molecules by removing water. |
| Hydrolysis | A chemical process that breaks down molecules by adding water. |
| Glycosidic Linkage | A covalent bond that joins carbohydrate monomers together. |
| Ester Linkage | A covalent bond that joins glycerol and fatty acids in lipids. |
| Peptide Bond | A covalent bond that links amino acids in proteins. |
| Phosphodiester Linkage | A covalent bond that links nucleotides in nucleic acids. |
| Monosaccharides | Simple sugars and the monomers of carbohydrates (e.g., glucose). |
| Disaccharides | Carbohydrates made of two monosaccharides linked together. |
| Polysaccharides | Long chains of monosaccharides used for energy storage or structure (e.g., starch, glycogen). |
| Saturated Fat | Fatty acids with only single bonds between carbon atoms; solid at room temperature. |
| Unsaturated Fat | Fatty acids with one or more double bonds; liquid at room temperature. |
| Denaturation | A change in protein shape caused by environmental factors like temperature or pH that stops protein function. |
| Enzyme | A protein that speeds up chemical reactions by lowering activation energy. |
| Activation Energy | The energy needed to start a chemical reaction. |
| Substrate | The reactant molecule that an enzyme acts upon. |
| Competitive Inhibitor | A molecule that binds to the active site of an enzyme, blocking the substrate. |
| Noncompetitive Inhibitor | A molecule that binds elsewhere on the enzyme, changing its shape and function. |
| What is the difference between anabolic and catabolic reactions? | Anabolic reactions build larger molecules and require energy, while catabolic reactions break down molecules and release energy. |
| Why is carbon so versatile in forming organic compounds? | Because carbon has four valence electrons allowing it to form four covalent bonds, leading to diverse structures like chains, branches, and rings. |
| What are the four main types of organic macromolecules? | Carbohydrates, lipids, proteins, and nucleic acids. |
| What elements are found in carbohydrates? | Carbon, hydrogen, and oxygen in a 2:1 hydrogen to oxygen ratio. |
| What is the monomer of proteins? | Amino acids. |
| What test detects monosaccharides? | Benedict's Solution. |
| What test detects polysaccharides? | Lugol's Iodine Solution. |
| What test detects proteins? | Biuret Solution. |
| What are the functional groups found in proteins? | Carboxyl (-COOH) and amino (-NH₂) groups. |
| What is the primary function of nucleic acids? | To store and transmit genetic information. |
| What is the difference between saturated and unsaturated fats? | Saturated fats have only single bonds and are solid at room temperature; unsaturated fats have double bonds and are liquid at room temperature. |
| How do enzymes affect activation energy? | They lower activation energy, speeding up chemical reactions. |
| What happens during dehydration synthesis? | Monomers are joined together by removing water molecules. |
| What happens during hydrolysis? | Polymers are broken down into monomers by adding water molecules. |
| How does a change from a hydrophobic amino acid to a hydrophilic one affect protein folding? | It can disrupt the folding process, especially during the tertiary stage, potentially causing improper folding and loss of protein function. |
| During which stage of protein folding do interactions between R groups primarily occur? | The tertiary structure stage. |
| What is the effect of protein denaturation on enzyme activity? | Denaturation changes the shape of the enzyme, preventing substrate binding and stopping the enzyme's function. |
| Why is the sequence of amino acids important in protein structure? | It determines the protein’s 3D shape and function; even a single amino acid change can alter folding and activity. |
| What role do enzymes play in anabolic and catabolic reactions? | They speed up both types of reactions by lowering activation energy, making cellular processes efficient. |
| How does temperature affect enzyme activity? | Moderate increases typically increase activity, but high temperatures can denature enzymes and stop function. |
| What is the difference between competitive and noncompetitive inhibitors? | Competitive inhibitors bind the active site blocking substrate; noncompetitive inhibitors bind elsewhere changing enzyme shape. |
| How do phosphodiester linkages contribute to nucleic acid structure? | They form the backbone by linking sugar and phosphate groups, creating stability and directionality. |
| Why is water necessary for hydrolysis reactions? | Water breaks covalent bonds between monomers, allowing polymers to be broken down. |
| What happens to enzyme activity when substrate concentration increases? | Activity increases until the enzyme becomes saturated and levels off. |
| How do changes in pH affect protein structure? | Extreme pH changes can disrupt hydrogen bonds and ionic interactions, leading to denaturation. |
| Why are lipids hydrophobic? | Because they have long hydrocarbon chains that are nonpolar and do not interact with water. |
| What is the importance of cholesterol in cell membranes? | It helps maintain membrane fluidity and stability. |
| How does the presence of double bonds in fatty acids affect fat properties? | Double bonds cause kinks, preventing tight packing and making fats liquid at room temperature. |
| How does dehydration synthesis relate to energy storage in macromolecules? | It forms bonds storing energy within larger molecules like starch or proteins. |
| Explain the role of minerals such as Zn, Mg, and Ca in organic organisms. | They act as cofactors for enzymes, structural components, and in signaling pathways. |
| How does a mutation in DNA affect protein production? | It can change the nucleotide sequence, potentially altering amino acid sequence and protein function. |
| What is the induced fit model of enzyme action? | Enzymes change shape slightly to fit substrates better, enhancing catalysis. |
| How do allosteric sites regulate enzyme activity? | Binding at allosteric sites changes enzyme shape and activity, allowing regulation. |
| Why is cellulose important in plants? | It provides structural support as a polysaccharide with beta linkages humans cannot digest. |
| What is ketosis and how do carbohydrates help prevent it? | Ketosis is the breakdown of fat for energy producing ketones; carbohydrates provide an alternative energy source preventing ketosis. |
Created by:
syeduvaka
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