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Chapter 3 Flashcards

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Biology 101 flashcards
1
Q

What type of chemical reaction occurs when monomers are joined to form polymers?

A

Polymerization

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2
Q

What type of chemical reaction occurs when polymers are broken apart into monomers?

A

Hydrolysis (water breaks down)

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3
Q

In which type of reaction is a water molecule released as a product of the reaction?

A

A water molecule released as a product of the reaction is dehydration synthesis. This chemical reaction means “to put together while losing water”

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4
Q

In which type of reaction is a water molecule broken apart so the reaction can go forward?

A

Hydrolysis

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5
Q

Which of the biological macromolecules is not a polymer?

A

Lipids

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6
Q

What features are shared by all carbohydrates?

A
  1. Carbon
    2.Hydrogen
    3.Oxygen
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7
Q

What is the ratio of carbons to hydrogens to oxygens in a carbohydrate molecule?

A

1:2:1

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8
Q

What are three ways in which monosaccharides can differ from one another?

A

1 the location of the carbonyl group
2 the number of carbon atoms they contain
3 orientations of their hydroxyl groups

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9
Q

For each of the following polysaccharides, describe 1) the type of monomer, 2) the type of glyosidic linkage, 3) branching (if any), 4) example organisms that have this type of polysaccharide, and 5) the major functions: starch, glycogen, cellulose, chitin, and peptidoglycan.

A
  1. Starch-plants store sugar as starch, can be broken down into glucose monomers (because it’s sugar), then it makes energy, bonds are easily broken, can be branched or unbranched, alpha glycosidic linkage
  2. Glycogen is animals storing sugar, can be broken down into glucose monomers bonds are easily broken, can be branched or unbranched, glycosidic linkage
  3. Cellulose- beta glycosidic linkage, polymers are unbranched, this is a structural polymer cell walls, parallel strands connected by hydrogen bonds
  4. Chitin- structural in fungi and exoskeletons of insects, parallel strands connected by hydrogen bonds, monomers modified by acetyl- amino acids
  5. Peptidoglycan-structural in bacteria cells walls, monomers modified by amino acids, parallel strands connected by peptide bonds
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10
Q

What are the four major functions that carbohydrates can perform in cells, and an example of each type?

A
  1. Energy storage- glycogen storage energy or form structures
  2. Energy production- glucose used for energy
  3. Building macromolecules- cellulose is string of glucose molecules
  4. Sparing Proteins - energy for the body
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11
Q

Both starch and cellulose are glucose polymers. Why can animals easily degrade starch, but not cellulose?

A

Animals don’t have the enzymes for it, they have a-glycosidic bonds but not b-glycosidic bonds

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12
Q

How can you tell from the molecular formula C6H10O5, that this six-carbon sugar is a disaccharide composed of two trioses and not a hexose?

A

Because their structure differs, chemically and structurally, they have different arrangements of the structural groups

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13
Q

What are some similarities between the structure of peptidoglycans, found in the cell walls of prokaryotes, and chitin, found in the exoskeletons of insects?

A

Both are for structural support, both are monomers.

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14
Q

How does the extensive hydrogen bonding found among parallel glucose polymers of cellulose contribute to its function in plants?

A

Cellulose holds and maintains the plant cells structure

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15
Q

What are the analogous functions of starch and glycogen and where are they stored in plants and animals?

A

Store energy for later, for plants its plastids, in animals its glycogen in skeletal muscles and liver

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16
Q

What are the properties and functions of the three major types of lipids: phospholipids, triglycerides and sterols (give example of each)?

A
  1. Phospholipids- lipid bilayers of a cell membrane
    2.Triglycerides-fats and oils
  2. Sterols- hormones like testosterone
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17
Q

What are several functions of fats in the body?

A
  1. Energy storage
  2. Cushioning and insulation
  3. Cell membrane component
  4. Precursors for certain vitamins
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18
Q

What is the structure of a triglyceride molecule?

A

There’s a glycerol and fatty acids
1. Fatty acids may contain double bonds
2. Bonds between carbon and unsaturated fats

19
Q

How do saturated and unsaturated fatty acids differ in their structure?

A
  1. Saturated is single bonded
  2. Unsaturated is double or more bonds
20
Q

What are some examples of saturated and unsaturated fats that are found in food?

A

1.Oil
2.Butter
3. Beeswax

21
Q

How do levels of saturated fats and cholesterol in the diet affect a person’s risk of developing cardiovascular disease?

A
  1. High level of trans fat can lead to bad cholesterol
  2. Can be lead to heart disease
  3. Too much is bad for you
22
Q

What is the molecular structure of phospholipids, and why do they spontaneously form bilayers in water?

A

Phospholipids safe a plasma membrane, two hydrophobic tails of fatty acids,has two layers (bilayers) make up cell membrane, they form in water because phospholipid head (are water loving) the tails doing because of they’re made up of fatty acids and oils, hydrophobic and hydrophilic interactions, they line up in the interior of the membrane

23
Q

What part of a phospholipid is hydrophilic and what part is hydrophobic?

A

The tails of a phospholipid is hydrophobic and the heads is hydrophilic.

24
Q

What structural features do all steroids have in common?

A

All have a four ring structure

25
Q

What are the functions of cholesterol in the body?

A

Important for plasma membrane and for steroid hormones.

26
Q

What are some examples of protein functions (give an example for each)?

A
  1. Catalyst : speeds up chemical reactions (ex: enzymes)
    2.Signaling : signal and receptor proteins exchange information (ex: testosterone, progesterone)
  2. Transport : Motor proteins transport materials around the cell; membrane proteins regulate what goes in/out of cell (ex: GLUT1, calcium ATPase)
  3. Gene Regulation : transcription regulator proteins bind to DNA to control gene expression (ex: activator proteins bind to regulatory sites)
  4. Fluid balance : serum proteins regulate distribution of fluid between blood and tissues (ex: Albumin and Globulin proteins)
  5. Structure : Cytoskeletal proteins define cell shape (ex: keratin, collagen)
  6. Movement : Motor and contractile proteins move the cell (ex: muscle protein Myosin motors the contraction of muscle fibers in animals)
27
Q

What structural features all amino acids have in common, and how are each of the 20 amino acids different from one another?

A

Amino acid R groups can be grouped into four general types: Acidic, basic, Uncharged Polar and Nonpolar. They differ based on the R group attached to the central carbon.

28
Q

What is an ionized amino acid, and where are you likely to find proteins with ionized amino acids?

A

Amino acids ionize in solutions such as water or bodily fluids; ionization results in the loss or gain of one electron, the molecule becomes electrically charged and more reactive with other molecules

29
Q

What are the features of a peptide bond, and what parts of amino acids are involved in making this bond?

A

A peptide bond is a condensation reaction (chemically joins two molecules together) that bonds the carboxyl group of one amino acid to the amino group of another amino acid.

30
Q

How do the amino acid side chains (R-groups) affect the biochemical properties of each amino acid?

A

The side chains affect the folding of the protein because it changes the unique sequence of amino acids in its primary structure, which ultimately determines its function

31
Q

Which are the biochemical characteristics of the amino acids that are in the following groups: nonpolar, polar uncharged, charged (acidic and basic)?

A

Non polar - hydrocarbon side chains are generally built from carbon and hydrogen, which have little electromagnetic difference; their results in bonds that are not polarized, or nonpolar
Polar uncharged - the hydroxyl group on Ser normally does not ionize, so it is not charged in proteins (it remains neutral)

32
Q

How do you identify the N-terminus and the C-terminus of a protein, and how are the amino acids in a protein numbered?

A

The N-terminus is part of the amino group and found at the start of the protein while the C-terminus is part of the Carboxyl group and found at the end of a protein. The amino acids are numbered based on its primary structure and the order of the peptide bonds found in the DNA sequence

33
Q

What are the four levels of protein structure?

A
  1. Primary - unique sequence of amino acids
  2. Secondary - formed by hydrogen bonds in the backbone of amino acid
  3. Tertiary - interactions between R groups and peptide backbone, which causes the 3D folding
  4. Quaternary - bonding of two or more distinct polypeptide units
34
Q

What biochemical characteristics of amino acids (carbon skeleton or side-groups) are important for the formation of protein secondary and tertiary structure?

A
  1. Secondary - Hydrogen bonds occur between the backbone of the carbonyl group of one amino acid and amino group of another
  2. Tertiary - R group interactions involved in protein folding include hydrogen bonds, hydrophobic interactions
  3. Covalent disulfide bonds, ionic bonds and Van der Waals interactions
35
Q
  1. What are the three basic parts of a nucleotide?
A
  1. Phosphates group
  2. Sugar
    3.Nitrogen base
36
Q

What is the importance of the 2’, 3’, and 5’ carbons of the sugar in the nucleotide?

A

Hydroxyl groups for on 3 and 5 carbons making a dna backbone (they link to a phosphate group)

37
Q

Which purines and pyrimidines are present in DNA and RNA?

A

Adenine, Guanine is the purines, the pyrimidines are Uracil (RNA) and Thymine (DNA).

38
Q

How do purines and pyrimidines hydrogen bond to each other to form complementary base pairs?

A

The shape allows them to bond together

39
Q

What is a nucleic acid, and what bond type connects nucleotides to one another within a nucleic acid strand?

A

Nucleic acid is the genetic blueprint, it carries the instruction so things can function

40
Q

What is meant by the 5’ end and the 3’ end of a DNA or RNA strand?

A

5 and 3 is the number of carbon atoms in deoxyribose sugar- a phosphate group bonds

41
Q

What is Chargaff’s rule for the ratios of nucleotides in a DNA sample, and how did this information help in solving the structure of the DNA molecule? If a sample of DNA has 30% guanine, how much adenine, thymine and cytosine does it have?

A

Chargaff rules was 2 empirical rules, one states purines= pyrimidines (A+G=C+T), and the second rule states A=T and C=G, this helped determine the structure because it showed that everything was in paris. Cytosine has 30, A=20 G=30 C=20 T=20.

42
Q

What are the primary and secondary structures of DNA?

A

Primary is ribose, secondary is polynucleic chains

43
Q

What are the primary, secondary, tertiary, and quaternary structures of RNA?

A

Primary=uracil, secondary= single stranded, has a loop like a bobby-pin,fold into complex shapes, tertiary= 3D, folds, building blocks, quaternary= multiple polypeptide chains

44
Q

How do DNA and RNA differ in their functions as information storage molecules in living organisms?

A

DNA stores the information, RNA is the messenger, under alkaline condition DNA is fine RNA is not

Bio (8 decks)

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