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Cell and Molecular Biology Exam 1
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Types of molecules that make up cells proteins (amino acids), carbohydrates (sugars), lipids, nucleic acids (DNA, RNA) Characteristics of all cells DNA, Inside/outside (cytoplasm/outside), membrane, RNA, proteins Differences between cells cellular organelles, shape (within/among), function (within/among) Cells vary in appearance and function, but they all have the same basic what? chemistry (central dogma: DNA>RNA>Proteins) Properties of life made of cells, sense and respond to stimuli, require energy for metabolism, reproduce, homeostasis (inside and outside), have metabolism Biological definition for homeostasis expending energy to maintain internal environment Who discovered cells and when? Robert Hooke in 1665 What did Schleiden and Schwann propose? cells compose all parts of plants and animals (1830s) Who (and how) was it discovered that cells did not spontaneously generate? Pasteur in the swan neck flask experiment in 1860s What did Virchow propose? cells grow and all cells arise from preexisting cells What are the 7 parts of modern cell theory?
Characteristics of prokaryotic cell ribosomes and DNA are in same compartment, so ribosomes convert RNA to proteins very quickly (fast protein synthesis), a membrane, simple cell plan Main organelles in eukaryotic cells (7) mitochondria, peroxisome, ER, golgi, nucleus, lysosome, vesicle Function of ER Protein and lipid synthesis. It also helps membranes grow or shrink to allow vesicles to move around cell Function of golgi package molecules from ER for secretion to another part of cell or excretion Function of nucleus store DNA info. double membrane with pores Function of lysosome break things down for intracellular digestion Function of mitochondria metabolism finishes here. Allows cells to take in O2. Outer and inner membrane. Uses surfaces area to increase metabolism. Has own DNA Function of peroxisome neutralizes oxidative toxins in cell and helps with some lipid synthesis How do prokaryotes accomplish the same metabolism as eukaryotes they do it across their outer membrane Cytosol everything in cell not inside lumen of organelles Cytoplasm everything inside a cell Size range of prokaryotic cells 0.5 micrometers-5 micrometers Size range of eukaryotic cells 10 micrometers-meters Four groups of molecules proteins, carbohydrates, lipids, nucleic acids Three groups of macromolecules
Draw an amino acid and label the ends Draw protein isomers Are proteins L-isomers or D-isomers? L-isomers What are covalent bonds in proteins called? peptide bonds What is the condensation reaction in a peptide bond? One OH from carboxyl end of an amino acid and an H from the amino end of an amino acid join to form H2O How many side chains are there? Are they molecules? Can they be charged?
Secondary structure (2°)? alpha helix or beta sheet or unstructured region. Don't rely on R group to form, and form via H-bonds in backbone atoms to hold. Characteristics of alpha helix (within 2°) Hydrogen bonds between amino and carboxyl groups of amino acids are four apart in sequence, R groups point out from helix, most are right-handed Characteristics of beta sheet (within 2°) multiple beta strands, hydrogen bonds between amino and carboxyl groups of adjacent beta strands, R groups point every other amino acid towards or away from adjacent strand. Can be parallel, anti-parallel Tertiary structure (3°)? The three 2° elements (alpha helices, beta sheets, unstructured regions) combine to make a 3D shape Quaternary structure (4°)? Organization of several peptides into one protein complex What is the purpose of chaperone proteins? sometimes (but not always) spontaneously folding will not be advantageous so chaperones interact with parts of protein to encourage specific folding What is the one kind of covalent bond that can form between R groups? disulfide bonds Characteristics of disulfide bonds formed between sulfur atoms of cysteine side group, redox reaction (LEO says GER), requires oxidizing conditions (in ER and outside cell, but not in cytosol) LEO says GER Lose electrons=oxidation, gain electrons=reduction What is an oxidizing environment? One that can accept electrons Protein domain Segment of a polypeptide chain that can fold into a compact stable structure and that usually carries out a specific function Coiled coil (Keratin) two alpha helices contact each other along their length How does elastin stretch?
To create order, disorder must be created elsewhere How do you know if disorder is being created? G is negative What are the four ways enzymes lower activation energy? stabilize transition state, bring two reactants together, alter electron distribution in the substrate, form temporary covalent bonds that change the reaction path What is an energetically unfavorable reaction? One whose G is positive How do enzymes allow cells to perform unfavorable reactions? by coupling it with a favorable reaction Will an energetically unfavorable reaction happen spontaneously? No What is a Michaelis constant? Is a low or high Michaelis constant better? Concentration of substrate at which enzymes works at half its maximum velocity Draw negative allosteric regulation. Label activity of each and on or off Draw positive allosteric regulation. Label activity of each and on or off What is feedback inhibition? Sort of negative allosteric regulation where end product of reaction reduces activity of enzyme early in pathway Does G change when reaction is catalyzed? no