Bio Final Flashcards
(233 cards)
Give a biological example for each property/processes associated with life that we covered in class. Give examples that are different from those in the book and used in class
- energy: they acquire and use energy ie. photosynthesis, respiration, fermentation, digestion
- cells: made up of membrane-bound units that regulate the passage of materials between exterior and interior spaces
- information: process hereditary / genetic information encoded in genes. ie. DNA, RNA
- replication: every organism replicates itself; reproduction
- evolution: organisms are the product of evolution, and populations continue to evolve; ie. giraffe with tongue that can eat thorny plants
In science, what is a hypothesis, and what is a theory? (see pages 7-8). How are they different?
hypothesis: testable statement to explain phenomena or observations – must be testable and falsifiable
theory: an explanation for a very general class of phenomena or observations that are supported by a wide body of evidence. Proposed explanations for broad patterns in nature
What is a “control” in an experiment? Why is it important?
checks for factors, other than the one being tested, that might influence the experiment’s outcome. (also controlling for the possibility that the manipulation itself affected the behavior)
What are the two components of cell theory?
- all living organisms are made of one or more cells ( You must have a cell in order to make another cell.)
- all cells come from preexisting cells (If you must have a cell to make another, then all cells must be related)
Approximately 96% of the human body is comprised of what four elements?
hydrogen, carbon, nitrogen, oxygen
What is the difference between a nonpolar and polar covalent bond?
- nonpolar covalent (ie. hydrogen molecule): electrons halfway b/t 2 atoms, shared equally;
- polar covalent (h2o); electrons shared unequally and one side is more electronegative and there’s partial charges on atoms; asymmetric sharing of electrons; Water is an example of a polar molecule. equal electronegativity between atom’s electrons that are shared equally or symmetrically -Oil is an example of an nonpolar molecule(this is why water and oil do not mix).
What is an isotope? Give two examples of how are isotopes are useful in the biological sciences.
isotopes (varying neutrons for the same element): most are stable. Isotopes are used in biology for carbon dating and radioactive tracers in things such as CAT scans.
specific heat capacity
he amount of energy required to raise the temperature of 1 gram of a substance by 1 degree Celsius; water has a high specific heat because hydrogen bonds must be broken before heat can be transferred and the water molecules begin to move faster. As molecules increase in overall polarity (and their ability to form hydrogen bonds), it takes an extraordinarily large amount of energy to change their temperature
surface tension
water organizes to maximize H bonds, breaking bonds requires energy ; enhanced attraction between the surface of water meniscus results in tension that minimizes the total surface area; when water molecules are at the surface, there are no water molecules above them for hydrogen bonding, they exhibit stronger attractive forces between their nearest molecules.
adhesion
attraction between unlike molecules, usually analyzed in regard to interactions between a liquid and a solid surface (water molecules adhere to glass and pull upward at perimeter) chalk on a chalkboard
cohesion
attraction between like molecules (water is cohesive because it stays toughener because of the hydrogen bonds that form between individual molecules); water molecules at surface form H bonds with water molecules and resist the upward pull of adhesion; allows capillary action – water attracted to objects with electric charge
why water is such an effective solvent:
both of the O-H bonds are polar, so the oxygen atom has a partial negative charge and hydrogen has a partial positive
molecule is bent —
the partial negative charge sticks out from the partial positive charges, giving it overall polarity
Using scientific terminology involving bonds and molecules, explain how salt dissolves in water.
hydration shells: negatively charged O side of water attracted to positively charged Na+ ion; and the positively charged side of water is attracted to the negatively charged Cl- ion.
Covalent bonds are stronger than ionic, so they’re more willing to form easily. They break ionic bonds and form covalent bonds.
e able to recognize the following functional groups (hydroxyl, carboxyl, carbonyl, sulfhydryl, methyl, phosphate, amino) listed in the table of your textbook and in your lecture notes. Look up the structure of estradiol, cysteine, and glucose and identify the functional groups in each.
OH Hydroxyl CH Methyl NH Amino SH Sulfhydryl
COO or CHOO Carboxyl CO or CHO Carbonyl
Phosphate PO (POOOO)
What is a polymer?
polymer: “many-parts” large number of monomers together
polymerization: linking monomers together = to form proteins
What type of chemical reactions add monomers together to form polymers? Are these reactions spontaneous or do they require energy?
monomers polymerize through condensation reactions (aka. dehydration reactions); requires energy – endergonic
What type of chemical reactions break polymers down into their monomer building blocks? Are these reactions spontaneous or do they require energy?
hydrolysis: breaks polymers apart by adding a water molecule, separating one monomer from the polymer chain (opposite of condensation reactions); dominates because it increases entropy and is favorable energetically; they do not require much energy = exergonic!
How are proteins denatured? What happens to the biological activity of a denatured protein and why?
denatured proteins: unfolded by treating with compounds that break hydrogen bonds and S-S bonds; it makes ribonuclease unable to function normally (ie. no longer break apart nucleic acids)
physical and chemical changes deactivate protein by denaturation (temp. pH, salt). ie. cook an egg, high fevers.
What are the four levels of protein structure (describe the different levels of structure)? What type of chemical bonds are responsible for each level?
rimary: sequence of amino acids
secondary: polypeptides form A-helix or B-sheets - H bonds in core structure
tertiary: interactions between amino acid side chains (curly) - unique folds b/c of covalent bonds, ionic bonds, H bonds, hydrophobicity, and van der Waals, R-groups
quaternary: complex, multiple subunits form function of protein b/c of covalent bonds, ionic bonds, H bonds, hydrophobicity, and van der Waals
What is the basic structure of an amino acid?
amino acid: building blocks of proteins / polypeptides, 20 types differ in side groups; All amino acids contain a Hydrogen. The examples are: H, NH2, COOH, and distinct side chains.
structure: include 1 amino group + carboxyl group, plus central carbon with hydrogen
Charged side chains (acidic or basic?): acidic = positive, basic = negative
R-group: polar or electronegatively charged side groups will react
amino acid = peptide
50 or less: oligopeptide
50+: polypeptide
when 50+ and functional = protein
What is a peptide bond?
peptide bond: bond responsible for linking monomers; bond forming between carboxyl group of one amino acid and the amino group of another; the C-N covalent bond resulting from a condensation reaction; very stable (compared to links in other types of macromolecules) because valence electrons on nitrogen is partially shared in the C-N bond — sharing is enough that bonds have characteristics of a double bond
carboxyl + amino group = peptide bond
aminos: act as base
carboxyl: acts as acid
Name 2 diseases associated with protein misfolding. For each of these diseases, explain the following:
What are the symptoms of this disease/disorder?
what protein is misfolded? How does misfolding affect the function of the protein in the cell?
how does misfolding contribute to the symptoms of this disease/disorder?
mad cow disease in cattle: PrP is a normal component of mammalian cells, but improperly folded version of the protein represents the infectious form of the prion
sponge-brain illnesses: sheep, cows, goats, and humans afflicted with these undergo massive degeneration of the brain; spongiform encephalopathy can be inherited and the disease is transmitted when individuals eat tissues containing the infectious form of PrP; all prion illnesses are fatal.
Alzheimers Disease: Symptom: confusion, memory loss. Misfolding proteins creates plaques that stick together. These plaques interfere with neurons in the brain, which eventually kills the neurons, resulting in memory loss. B-amyloid precursor protein APP: transmembrane protein in brain 40aa highly processed, B-deposits cause plaque to form in brain; neurofibrillary tangles – microtubule stability – progressive loss of synaptic connections
What are chaperone proteins? Why are they important in the cell
chaperonins: aid in protein folding:
unfolded protein enters cylinder
cap attaches, cylinder changes shape (hydrophobic inside now!)
cap comes off, protein released
What is an enzyme? How do they work
enzyme: a protein that functions as a catalyst; enzymes also: lock and key — enzymes are lock and keys are substrates that fit into the lock and react