Unit 1 Flashcards

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1
Q

What is a covalent bond?

A

The sharing of a pair of valence electrons by two atoms, which can be of the same or different elements. In a covalent bond, the shared electrons count as part of each atom’s valence shell. In nonpolar covalent bonds, electrons are shared equally since the electronegativity of the atoms is similar. In polar covalent bonds, electrons are drawn toward the more electronegative atom, resulting in dipoles.

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2
Q

What is a hydrogen bond?

A

A hydrogen bond forms when a hydrogen atom covalently bonded to one electronegative atom is also attracted to another electronegative atom (only Nitrogen, Oxygen, and Fluorine).

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3
Q

What are Van der Waals Interactions?

A

Electrons are not evenly distributed, and they may accumulate by chance in one part of a molecule based on their random movement, resulting in dipoles.
Van der Waals interactions are attractions between molecules that are close together as a result of these charges.

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4
Q

What are the four emergent properties of water?

A

cohesion, moderating temperature, expansion upon freezing, and solvent versatility

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5
Q

How does hydrogen bonding contribute to cohesion? What are the benefits of cohesion?

A

Hydrogen bonding holds H2O together through the attractions of opposite dipoles. Hydrogen bonds are constantly broken and reformed, so many molecules could be linked through them, which makes this liquid more structured. This gives a strong surface tension since, at the border between air and water, the surface of the water is hydrogen-bonded together but not to the air, resulting in asymmetry. The surface tension allows plants and animals to float and cohesion allows for the transfer of nutrients and water in plants.

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6
Q

How does hydrogen bonding contribute to moderating temperature?

A

Water is able to absorb heat from warm air and can release heat to cold air without a large change in the water temperature. This is because of water’s high specific heat caused by hydrogen bonding. Absorbing heat initially breaks hydrogen bonds, resulting in a low change in temperature. Since the energy is first used to break bonds before H2O moves faster and increases its thermal energy.

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7
Q

What are the benefits of water moderating temperature?

A

Water’s high specific heat allows coastal land to be heated at night and cooled during the day. The heat of vaporization allows for tropical seas to absorb heat via evaporation. This water then goes to the poles and releases heat when it condenses to rain. Evaporative cooling means that as the liquid evaporates, the surface of a liquid that remains is cool because the hottest molecules with higher KE already evaporated, which prevents overheating (sweating). This is why animals are mostly water.

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8
Q

How does hydrogen bonding contribute to expansion upon freezing? What are the benefits of this?

A

At 0 C H2O forms lattice structures that keep hydrogen bonds and molecules far enough to be less dense than H2O. If ice sank, then bodies of water could potentially freeze over. Ice also helps insulate the water underneath and keeps organisms there alive.

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9
Q

How does hydrogen bonding contribute to solvent versatility?

A

Water is a very polar molecular, which makes it a great solvent. Its charged dipoles attract the solutes and shield their polar/ionic attractions.

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10
Q

Describe, and rank by force of attraction, the following intermolecular bonds and forces:
Ionic
Hydrogen bonds
London forces

A

Ionic bonds are an attraction between a cation and anion. These bonds are formed as a result of the ions’ charges not just due to the act of a highly electronegative atom stealing electrons. Ionic bonds are the strongest of the three forces because their attractions are based on set oppositely charged ions rather than partial charges. Hydrogen bonds are the next strongest because the partial charges are not random but as a result of the electronegativities of the atoms, which allows for some consistencies. London dispersion forces are based on the random movement of electrons that may result in a temporary high density of electrons in one area that forms a dipole.

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11
Q
Identify and draw the following functional groups
Hydroxyl
Carbonyl
Carboxyl
Amino
Sulfhydryl
Phosphate
Methyl
A

Hydroxyl, carbonyl, carboxyl, amino, sulfhydryl, and phosphate are all reactive. Of these, only sulfhydryl is not hydrophilic. Methyl is used as a recognizable tag on biological molecules.

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12
Q

Identify the four categories of biological macromolecules.

A

carbohydrates, proteins, nucleic acids, and lipids

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13
Q

What are carbohydrates?

A

These include sugars and polymers of sugars.

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14
Q

What are monosaccharides?

A

the simplest carbs that builds more complex ones. These are usually a multiple of CH2O. Its trademarks are carbonyls and multiple OH groups. The size is usually 3-7 carbons long. In aqueous solution 5-6 C sugars form rings since they are the most stable. Ex. glucose

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15
Q

What is a disaccharide?

A

2 monosaccharides joined by a glycosidic linkage. These molecules must be broken down into monosaccharides to be used for energy. Ex. maltose/sucrose

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16
Q

What is a glycosidic linkage?

A

a covalent bond formed between two monosaccharides by a dehydration reaction

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17
Q

What are polysaccharides?

A

macromolecules; polymers with a few hundred to a few thousand monosaccharides joined by glycosidic linkages. These serve as storage material for energy later like starch in plants and glycogen in animals. They are also used as building protective structures like chitin in exoskeletons and cellulose in plants.

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18
Q

Illustrate the dehydration synthesis.

A

Dehydration synthesis is a type of condensation reaction that connects monomer to monomer or to a polymer with covalent bonds that results in the loss of a water molecule. This synthesis is found in carbon and protein polymer formation.

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19
Q

Illustrate hydrolysis.

A

Polymers are disassembled by hydrolysis, which breaks the bonds of monomers by adding water. An H is added to one monomer and an OH is added to the other. This occurs in digestion with enzymes.

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20
Q

Explain the biological significance of alpha vs beta glycosidic bonds and 1-4 vs 1-6 linkages in polysaccharides.

A

When glucose forms a ring, the hydroxyl group attached to the number 1 carbon is positioned either below or above the plane of the ring. These two ring forms for glucose are called alpha (a) and beta
(b), respectively. In starch, all the glucose monomers are on the same orientation with 1-4 links (a) In contrast, the glucose monomers of cellulose are all in the b configuration, making every glucose monomer “upside down” with respect to its neighbors.
The differing glycosidic linkages in starch and cellulose give the two molecules distinct three-dimensional shapes and therefore different functions. Certain starch molecules are largely helical, fitting their function of efficiently storing glucose units. Conversely, a cellulose molecule is straight. Cellulose is never branched, and some hydroxyl groups on its glucose monomers are free to hydrogen-bond with the hydroxyls of other cellulose molecules lying parallel to it. These cable-like microfibrils are a strong building material for plants.
Enzymes that digest starch by hydrolyzing its a linkages are unable to hydrolyze the b linkages of cellulose due to the different shapes of these two molecules.

The alpha-1,4-glycosidic bond is the more common bond and it gives glycogen a helical structure that is suitable for energy storage. The alpha-1,6-glycosidic bond bonds are found about every ten or so sugars and these create branching points.

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21
Q

What is a protein?

A

a biologically functional molecule made up of 1 or more polypeptides, each folded and coiled into a specific 3D structure.

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22
Q

What are the functions of proteins?

A

enzymatic, defensive, storage, transport, hormonal, contractile and motor, structural, and receptor proteins

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23
Q

What are proteins made of and how are they formed?

A

Proteins are composed of amino acids as their building blocks. Bonds between amino acids are peptide bonds that form polypeptides, a polymer of amino acids. A peptide bond is a covalent bond formed when two amino acids are positioned so that one carboxyl is adjacent to the amino group of another, and they become joined via a dehydration reaction.

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24
Q

What determines the functions of proteins?

A

the R groups of amino acids have different physical and chemical properties that determine the characteristics of amino acids and thus the function of the polypeptide. The R groups also determine the protein’s structure, which is how it works since it needs to recognize and bind to other molecules

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25
Q

Define an amino acid.

A

an organic molecule with amino and a carboxyl group

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26
Q

How are the amino acids grouped?

A

Amino acids are group based on the R group.
nonpolar R group- hydrophobic; Ex. R group = CH3-R
polar R group- hydrophilic; Ex. R group = OH-CH2-R
acidic group- have R groups w/ (-) charge due to carboxyl group, which is ionized at cell pH; R has COOH
basic group- have R groups with (+) charge; R has NH3+ at 7 pH

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27
Q

Draw the generic structure of amino acids and peptide bonds.

A
amino acid:     
         R
          |
H2N-C- C=O
          |    |
         H OH
peptide bond:
        R   O
         |    ||
H2N-C-C-N-C-C=O
         |     |      |   |
        H    H   H OH
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28
Q

What is a primary structure?

A

Protein’s sequence of amino acids; determines the secondary and tertiary structure due to the chemical nature of the backbone and R groups.

29
Q

What are the secondary structures?

A

Most proteins have segments of repeated coiling/folded patterns contributing to the overall shape as a result of H bonds between repeating constituents of the backbone. In the backbone, O has partial negative and H on N has partial positive.

alpha helix- delicate coil held by H bonding between every fourth amino acid
beta-pleated sheet: two plus segments of polypeptide chain lying side by side connected by H bonds between two parts of parallel segments

30
Q

What are tertiary structures?

A

The overall shape of polypeptides resulting from interactions between R groups of various amino acids.
Some examples are hydrophobic interactions, which is as the polypeptide folds, amino acids with nonpolar groups end up in clusters away from water. Disulfide bridges have 2 cysteine monomers with SH as R are brought close together by folding to form an S-S-S bridge.

31
Q

What are quarternary structures?

A

the overall structure resulting from the aggregation of polypeptides; a protein with 2 or more polypeptide chains

32
Q

Define denaturation

A

if pH, salt concentrations, temperature, and other environmental changes occur, the weak chemical bonds and interactions in protein may be destroyed, causing it to unravel and lose its native shape

33
Q

What are lipids?

A

a diverse group of hydrophobic molecules because they consist of mostly nonpolar C-H bonds; the three kinds are fats, phospholipids, and steroids

34
Q

What are fats?

A

fats are not polymers but are assembled via a dehydration reaction resulting in ester linkage between OH and COOH; they consist of glycerol (alcohol with an OH on each of its 3 Carbon atoms) joined to 3 fatty acids (long carbon skeleton, usually 16-18 C in length with COOH at the end; the major function of fats is energy storage

35
Q

What is the difference between saturated and unsaturated fatty acids?

A

saturated fatty acids do not have any double bonds between carbons in the chain while unsaturated fatty acids have 1+ double bonds, resulting in fewer hydrogen atoms

36
Q

What is a phospholipid?

A

2 fatty acids attached to glycerol. The 3rd hydroxyl of glycerol is joined to a phosphate group with a negative electrical charge, typically another small charged/polar molecule is linked to a phosphate group

37
Q

What is a steroid?

A

lipids characterized by a carbon skeleton consisting of 4 fused rings Ex. cholesterol; different steroids are distinguished by groups attached to rings

38
Q

What is the difference between pyrimidine and purine nitrogenous bases?

A

Pyrimidines are one 6 membered rings of carbon and nitrogen atoms. Thymine, cytosine, and uracil are examples. Purines are larger with 6 membered rings fused to a 5 membered ring. Guanine and adenine are purines. Specific nitrogenous bases differ based on the attached chemical groups.

39
Q

What are nucleic acids?

A

Nucleic acids store, transmit, and help express hereditary information. RNA and DNA are the two types of nucleic acids. Nucleic acids are polymers of monomers, called nucleotides. The links between nucleotides are phosphodiester linkage, resulting in a sugar-phosphate backbone and nitrogenous bases as appendages. This is a condensation reaction.

40
Q

What are nucleotides composed of?

A

Nucleotides are made of a 5 carbon sugar, nitrogen-containing base, and 1-3 phosphate groups

41
Q

Describe the differences between RNA and DNA.

A

DNA has the sugar deoxyribose and RNA has ribose. DNA has 2 polynucleotide strands forming a double helix with the sugar-phosphate backbonds running in opposite directions (antiparallel) held by hydrogen bonds and the two strands complementary with the order of NBs. RNA is only one strand and can have variable shapes.

42
Q

Identify the components of cell membranes, and explain how the arrangement of components makes the membrane semi-permeable.

A

Cell members follow the fluid mosaic model with the membrane as a mosaic of protein molecules bobbing the fluid bilayer. The phospholipid bilayer is what makes the membrane semipermeable since the phospholipid tails are nonpolar and the heads are polar. Therefore, nonpolar molecules can pass through more easily. However, the transport proteins dotting the membrane allow for the passage of hydrophilic substances to cross the membrane via simple/facilitated diffusion.

43
Q

Describe diffusion.

A

movement of particles of any substance so that they spread out into the available space down its concentration gradient.

44
Q

Describe passive transport.

A

diffusion of a substance across a membrane without energy investment.

45
Q

Describe facilitated diffusion.

A

transport proteins speed the passive movement of molecules across the plasma membrane; polar molecules/ions diffuse passively with the help of transport proteins that span the membrane.
Transport proteins include channel proteins and carrier proteins. Channel proteins provide an avenue to allow specific molecules to pass through.

46
Q

Describe mediated diffusion.

A

Refers to both facilitated diffusion and active transport. Other transport proteins, called carrier proteins, bind to molecules and change shape to shuttle them across the membrane for active transport after a conformation change resulting from ATP energy transfer. Channel proteins help with facilitated diffusion.

47
Q

Define the following terms, and explain how they relate to the movement of materials across a membrane:
Isotonic
Hypotonic
Hypertonic

A

Tonicity is the ability of a surrounding solution to cause a cell to gain or lose water depending on the concentration of solutes that cannot cross the membrane relative to inside the cell. In isotonic solutions, there is no net movement of water across the membrane (equal concentration). In hypertonic solutions, the cell will lose water and shrivel since the outside of the cell has a higher concentration of solute. In hypotonic solutions, water will enter the cell faster than it leaves and swells and lyses because the solute concentration is lower outside the cell.

48
Q

Describe active transport.

A

uses energy (usually ATP) to move solutes against their concentration gradient, which is carried out by only carrier proteins. This helps the cell maintain an internal concentration different than the external. Ex. sodium/potassium pump

49
Q

Explain how larger objects/molecules cross membranes by exocytosis and endocytosis and predict when each of these transport mechanisms is used.

A

Exocytosis is when cells secrete molecules by the fusion of vesicles with the plasma membrane while endocytosis is when the cell takes in molecules and particulate matter by forming new vesicles from the plasma membrane. There are 3 kinds of endocytosis: phagocytosis, pinocytosis, and receptor-mediated endocytosis.

50
Q

What is phagocytosis?

A

AKA “cellular eating”: cells engulf particles by extending pseudopod is around them and packaging them within a membranous sac called a food vacuole. The particle is digested after the vaculoe fuses with a lysosome.

51
Q

What is pinocytosis?

A

AKA “cellular drinking”: cells continually “gulps” droplets of extracellular fluid into tiny vacuoles formed by infoldings of plasma membranes. The cell obtains nonspecific molecules dissolved in the droplets.

52
Q

What is receptor-mediated endocytosis?

A

specialized pinocytosis enabling cells to acquire a bulk of specific quantities. Solutes bind to receptor proteins which cluster to form a vesicle

53
Q
Predict how the following conditions affect membrane transport:
gradient conditions
temperature
ATP availability
changes in permeability
molecule size, charge, or polarity
A

If there is a small difference in gradients, then diffusion will be slow until there is no net movement. If the cell needs to maintain a certain concentration that is not already established through isotonic conditions, it will need to expend energy to force the desired concentration.

Temperature increases the rate of diffusion because it excites molecules with thermal energy, which therefore increases its kinetic energy and movement. The opposite case for lower temperatures. However, if the temperature increases too much, then the phospholipids will spread out in the membrane too much and greatly increase transport. Decreasing the temperature will cluster the phospholipids together and make them less permeable and slow down the rate of diffusion.

ATP availability affects active transport. If there is not enough energy to supply carrier proteins, then the conformational change of the protein will not occur, and active transport will slow down until there is no more energy left.

Larger, polar molecules will diffuse across the membrane slowly or not at all without the help of transport proteins. In general, Increasing the molecular size or charge/polarity has the same effect.

54
Q

Nucleus

A

The nucleus contains most of the DNA in a eukaryotic cell
The nucleus contains most of the cell’s genes and is usually the most conspicuous organelle
The nuclear envelope encloses the nucleus, separating it from the cytoplasm

55
Q

Mitochondria

A

Mitochondria are the sites of cellular respiration, a metabolic process that uses oxygen to
generate ATP
Mitochondria are found in nearly all eukaryotic cells
They have a smooth outer membrane and an inner membrane folded into cristae
The inner membrane creates two compartments: intermembrane space and mitochondrial matrix
Some metabolic steps of cellular respiration are catalyzed in the mitochondrial matrix
Cristae present a large surface area for enzymes that synthesize ATP

56
Q

Chloroplasts

A

found in plants and algae, are the sites of photosynthesis
Chloroplasts contain the green pigment chlorophyll, as well as enzymes and other molecules that function in photosynthesis
Chloroplasts are found in leaves and other green organs of plants and in algae
Chloroplast structure includes
Thylakoids, membranous sacs, stacked to form a granum
Stroma, the internal fluid
The chloroplast is one of a group of plant organelles, called plastids

57
Q

Ribosomes

A

are complexes made of ribosomal RNA and protein
Ribosomes carry out protein synthesis in two locations:
In the cytosol (free ribosomes)
On the outside of the endoplasmic reticulum or the nuclear envelope (bound ribosomes)

58
Q

Rough and Smooth Endoplasmic Reticulum

A

The endoplasmic reticulum (ER) accounts for more than half of the total membrane in many eukaryotic cells
The ER membrane is continuous with the nuclear envelope
There are two distinct regions of ER:

Smooth ER, which lacks ribosomes
Synthesizes lipids
Metabolizes carbohydrates
Detoxifies drugs and poisons
Stores calcium ions

Rough ER, whose surface is studded with ribosomes
Has bound ribosomes, which secrete glycoproteins (proteins covalently bonded to carbohydrates)
Distributes transport vesicles, secretory proteins surrounded by membranes
Is a membrane factory for the cell

59
Q

Vesicles

A

sacs made of the membrane (used for transport of materials in and out of the cell)

60
Q

Golgi apparatus

A

The Golgi apparatus consists of flattened membranous sacs called cisternae
The Golgi apparatus
Modifies products of the ER
Manufactures certain macromolecules
Sorts and packages materials into transport vesicles

61
Q

Cell Membrane

A

a selective barrier that allows passage of enough oxygen, nutrients, and wastes to service the entire cell

62
Q

Cytoplasm

A

the region between the nucleus and plasma membrane in which proteins/organelles are suspended in the cytosol

63
Q

Cell Wall

A

the outer layer that maintains the cell’s shape (plant) and protects the cell from mechanical damage; made of cellulose, other polysaccharides, and protein

64
Q

Vacuoles

A

Vacuoles are large vesicles derived from the ER and Golgi apparatus
Vacuoles perform a variety of functions in different kinds of cells
Food vacuoles are formed by phagocytosis
Contractile vacuoles, found in many freshwater protists, pump excess water out of cells
Central vacuoles, found in many mature plant cells, hold organic compounds and water

65
Q

Lysosomes

A

A lysosome is a membranous sac of hydrolytic enzymes that can digest macromolecules
Lysosomal enzymes work best in the acidic environment inside the lysosome
Hydrolytic enzymes and lysosomal membranes are made by rough ER and then transferred to the Golgi apparatus for further processing
Some types of cell can engulf another cell by phagocytosis; this forms a food vacuole
A lysosome fuses with the food vacuole and digests the molecules
Lysosomes also use enzymes to recycle the
cell’s own organelles and macromolecules,
a process called autophagy

66
Q

Cytoskeletal elements

A

reinforces the cell’s shape; functions in cell movement; components are made of proteins. includes microfilaments, intermediate filaments, and microtubules.

67
Q

Identify which cell components are found in:
all cells
prokaryotes (Eubacteria, Archaea)
eukaryotes (Animals, Plants, Protists, Fungi)

A

all cells- Plasma membrane, Semifluid substance called cytosol, Chromosomes (carry genes), Ribosomes (make proteins)
prokaryotes- No nucleus, DNA in an unbound region called the nucleoid, No membrane-bound organelles, Cytoplasm bound by the plasma membrane
eukaryotes- DNA in a nucleus that is bounded by a double membrane, Membrane-bound organelles, Cytoplasm in the region between the plasma membrane and nucleus, Eukaryotic cells are generally much larger than prokaryotic cells

68
Q

Predict the possible functions of an unknown cell depending on its components.
Predict the abundance of particular organelles depending on a cell’s functions.

A

Higher activity of lysosomes followed by initial higher activity of ER and GA could mean the cell were macrophages. These immune system cells have many lysosomes for the destruction of bacteria and other invaders brought into the cell via phagocytosis. The enzymes (hydrolases) that carry out this catabolic activity are synthesized in the endoplasmic reticulum, modified in the Golgi, and transported to the lysosomes. Cells that are in charge of producing energy might have more mitochondria or chloroplasts. Similarly, cells in charge of producing enzymes might have more activity in rough ER/ribosomes and the GA. Detox cells like in the cells might see more action in the smooth ER.