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Week 2 Study Guide
Week 2 Study Guide. LECTURES 3-5. UC MERCED Bio 011
| Question | Answer |
|---|---|
| Describe the general structure of atoms. | Atoms consist of 3 basic particles: protons, electrons, and neutrons. The nucleus (center) of the atom contains the protons (+) and the neutrons (no charge). The outermost regions of the atom are called electron shells and contain the electrons (-). |
| Which of the following is likely to involve a polar bond? | Cl-Cl, C-F, O-O and C-H...Answer is C-F because the electronegativity Fluorine is one of the most electronegative element. |
| Which is the most likely pathway taken by a newly synthesized protein that will be secreted by a cell? | ER --> Golgi --> vesicles that fuse with plasma membrane |
| List the elements that make up most of the mass of all living organisms. | The elements that are present in the highest quantities in living organisms are oxygen, carbon, hydrogen, nitrogen, sulfur, and phosphorus. |
| Explain the concept of Electronegativity | A measure of an atom's ability to attract shared electrons to itself. |
| Describe how a molecule’s SHAPE is important to its ability to interact with other molecules. | The shape affects the polarity because it determines how the positive and negative ends of the bonds line up. If they cancel out, the molecule is nonpolar. If they don’t, the molecule is polar. |
| Describe how hydrogen bonding determines many properties of water. | The shape of the water molecule is like a V. The negative end of one molecule is attracted to the positive end of another molecule. This is called hydrogen bonding. Hydrogen bonding is like a strong glue that holds water molecules together. |
| List the properties of water that make it a good solvent | Water is a good solvent b/c it can dissolve many polar and ionic substances. ex. nutrients, minerals etc. |
| Discuss the properties of water that are critical for the survival of living organisms. | High specific heat capacity, polar molecule, has a high heat of vaporization, strong adhesive forces, meaning it can stick to itself and to other surfaces. |
| Explain the properties of carbon that make it the chemical basis of all life. | can make reactive molecules. it's also small n easy 2 move around, which helps living things do chemical reactions. makes complex molecules, like DNA & RNA, which carry the instructions 4 life. |
| Explain dehydration reactions and how hydrolysis reactions reverse this process. | D.R's move water from small molecules (called monomers) to link them into larger molecules (called polymers). H.R's add water to large molecules (called polymers) to split them into smaller molecules (called monomers). |
| Carbohydrates | Biological molecules made of carbon, hydrogen, and oxgen in a ratio of roughly 1 carbon atom : 1 water. Divided into 3 main types depending on # of sugar units they contain. |
| Why is shape of a protein important for its function? | B/c it determines how the protein interacts w/ other molecules, like substrates, enzymes, receptors, & antibodies. If the shape of a protein is altered by factors such as temp., pH, or mutations, the protein may lose its function or become harmful. |
| List the classes of lipid molecules important in living organisms. | Fats and oils: used for energy storage, insulation, and protection of vital organs. Phospholipids:amphipathic =have both hydrophilic & hydrophobic regions. This allows them to form bilayers that are the main component of cell membranes. |
| Explain why phospholipids form a bilayer when dissolved in water. | Phospholipids have a hydrophilic head & a hydrophobic tail. When they r in water, they form a double layer w/ the heads facing the water & the tails hiding from the water. This is called the lipid bilayer, and it is the main structure of cell membranes. |
| Describe how amino acids are joined to form a polypeptide. | Amino acids r joined to form a polypeptide by peptide bonds, which link the amino group of one amino acid to the carboxyl group of another. This releases a water molecule and creates a chain of amino acids. |
| Explain the 1st and 2nd levels of protein structure | Primary structure of a protein is the sequence of amino acids in a polypeptide chain. Secondary structure of a protein is the local folding or coiling of the polypeptide chain into regular patterns, |
| Describe the three components of a nucleotide. | Has three components: a nitrogenous base, a pentose sugar, and a phosphate group |
| Explain the importance of hydrogen bonding in DNA and RNA. | Holds complementary base pairs together in the double helix of DNA. Allows DNA to separate & rejoin during replication & transcription. Facilitates the recognition & binding of enzymes |
| How does electronegativity contribute to the formation of polar and nonpolar covalent bonds? | Polar covalent bonds result when electrons are unequally shared between atoms, while nonpolar covalent bonds result when electrons are more equally shared between atoms. |
| Describe how a molecule’s POLARITY is important to its ability to interact with other molecules. | molecule is group of atoms stuck together by sharing/stealing electrons. Some atoms r more greedy than others, so they pull electrons closer to themselves. This makes one end of the bond more negative and the other more positive. This is called polarity. |
| What are some of the properties of water that are determined by hydrogen bonding ? | High boiling point and heat capacity, Cohesion and adhesion, Surface tension and Density and ice formation |
| Distinguish between hydrophilic and hydrophobic substances. | Hydrophilic substances are those that are attracted to water and can dissolve or disperse in it. Hydrophobic substances are those that repel water and are not soluble in it. |
| Ionic bonds | Elements gain or lose electrons to have a full outermost shell |
| Covalent Bonds | Elements share electrons to have a full outermost shell |
| Van der Waals forces | Weak interactions between molecules that are very close together; important for protein 3D structure |
| Functional groups: | Small groups of atoms with specific chemical properties |
| Isomers | Molecules with the same atoms and functional groups but different structures |
| Structural isomers: | different arrangement of atoms = different properties |
| Stereoisomers: | differrent in 3D geometry = different properties |
| Carbohydrates | Sugars that provide energy and structure for cells. Made of monosaccharides, which can join to form polysaccharides, such as starch, glycogen, and cellulose. |
| Lipids | Fats that store energy and form membranes and hormones. Made of fatty acids & glycerol, which can combine to form triglycerides, phospholipids, and steroids. |
| Proteins | Molecules that perform various functions in cells, such as catalysis, transport, signaling, defense, & movement. Made of amino acids, which can link to form polypeptides, which can fold into different shapes and structures. |
| Nucleic acids | Molecules that store and transfer genetic information. Made of nucleotides, which have a sugar, a phosphate, and a base. They can form DNA and RNA, which can encode and express genes. |
| What 3 main types can carbohydrates be divided into? | Monosaccharides, Disaccharides and Polysaccharides |
| Explain the 3rd level of protein structure: | Tertiary structure of a protein is the 3D shape of the polypeptide chain, which results from various interactions between the amino acid side chains, or R groups |
| 4th level of protein structure: | Quaternary structure of a protein is the association of two or more polypeptide chains into a functional protein. |
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