Chapter 5 - The Structure and Function of Large Biological Molecules Flashcards

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1
Q

All living things are made up of these four classes of large biological molecules:

A
  • carbohydrates
  • lipids
  • proteins
  • nucleic acids
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2
Q

Macromolecules

A

large molecules composed of thousands of covalently connected atoms.

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3
Q

polymer

A

A long molecule consisting of many similar or identical monomers linked together by covalent bonds.

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4
Q

monomer

A

The subunit that serves as the building block a polymer

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5
Q

dehydration reaction

A

occurs when two monomers bond together through the loss of a water molecule.

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6
Q

hydrolysis

A

Polymers are disassembled to monomers. Hydrolysis adds a water molecule, breaking a bond.

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7
Q

Carbohydrates

A

include sugars and the polymers of sugars. Though often drawn as linear skeletons, inaqueous solutions many sugars form rings.

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8
Q

monosaccharides

A
  • The simplest carbohydrates.
  • Also known as “single sugars”.
  • have molecular formulas that are usually multiples of CH₂O
  • Glucose (C₆H₁₂O₆) is the most common monosaccharide
  • serve as a major fuel for cells and as raw material for building molecules
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9
Q

Monosaccharides are classified by…

A
  • The location of the carbonyl group (as aldose or ketose)
  • The number of carbons in the carbon skeleton
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10
Q

polysaccharides

A
  • A polymer of many monosaccharides, formed by dehydration reactions.
  • The polymers of sugars have storage and structural roles.
    • Structure and function determined by its sugar monomers and the positions of glycosidic linkages
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11
Q

disaccharide

A

A double sugar, consisting of two monosaccharides joined by a glycosidic linkage formed by a dehydration reaction.

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12
Q

Glycosidic linkage

A

A covalent bond formed between two monosaccharides by a dehydration reaction.

  • Polymers with α glucose are helical
  • Polymers with β glucose are straight
    • H atoms on one strand can bond with OH groups on other strands
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13
Q

Starch

A

A storage polysaccharide in plants, consisting entirely of glucose monomers joined by α glycosidic linkages.

  • Plants store surplus starch as granules within chloroplasts and other plastids
  • The simplest form of starch is amylose
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14
Q

Glycogen

A

An extensively branched glucose storage polysaccharide found in the liver and muscle of animals; the animal equivalent of starch.

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15
Q

Cellulose

A

A structural polysaccharide of plant cell walls, consisting of glucose monomers joined by β glycosidic linkages. In these β structures, H atoms on one strand can bond with OH groups on other strands. Parallel cellulose held together this way are grouped into microfibrils, which form strong building materials for plants.

  • Cellulose is a major component of the tough wall of plant cells
  • Like starch, cellulose is a polymer of glucose, but the glycosidic linkages differ
    • Difference is based on two ring forms for glucose: alpha (α) and beta (β)
  • Enzymes that digest starch by hydrolyzing α linkages can’t hydrolyze β linkages in cellulose
    • Passes through the digestive tract as insoluble fiber, or like in many herbivores, microbes use enzymes to digest the cellulose.
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16
Q

Chitin

A

A structural polysaccharide, consisting of amino sugar monomers, found in many fungal cell walls and in the exoskeletons of all arthropods.

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17
Q

Lipids

A

Any group of large biological molecules, including fats, phospholipids, and steroids, that mix poorly, if at all, with water.

  • Do not form polymers
  • Lipids are hydrophobic because they consisty mostly of hydrocarbons, which form nonpolar covalent bonds.
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18
Q

Fat

A

A lipid consisting of three fatty acids linked to one glycerol molecule; also called a triacylglycerol or triglyceride.

  • Fats separate from water because water molecules form hydrogen bonds with eachother and exclude the fats
  • In a fat, three fatty acids are joined to glycerol by an ester linkage, creating a triacylclycerol, or triglyceride.
    • Ester linkage: any of a class of compounds produced by reaction between acids and alcohols with the elimination of water. Esters with low molecular weights, such as ethyl acetate, are usually volatile fragrant liquids; fats are solid esters
  • The major function of fats is energy storage
    • Humans and other mammals store their fat in adipose cells
      • Adipose tissue also cushions vital organs and insulates the body
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19
Q

Glycerol

A

A three-carbon alcohol with a hydroxyl group attached to each carbon.

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20
Q

Fatty Acid

A

A carboxylic acid with a long carbon chain. Fatty acids vary in length and in the number and location of double bonds; three fatty acids linked to a glycerol molecule form a fat molecule, also known as a triacylglycerol or triglyceride.

  • Fatty acids vary in length (number of carbons) and in the number and locations of double bonds.
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21
Q

Saturated fatty acid

A

A fatty acid in which all carbons in the hydrocarbon tail are connected by single bonds, thus maximizing the number of hydrogen atoms that are attached to the carbon skeleton.

  • Solid at room temperature
  • Most animal fats are saturated
  • Diets rich in this may contribute to cardiovascular disease through plaque deposits
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22
Q

Unsaturated fatty acids

A

A fatty acid that has one or more double bonds between carbons in the hydrocarbon tail. Such bonding reduces the number of hydrogen atoms attached to the carbon skeleton.

  • Also known as oils because they are liquid at room temperature
  • Plant fats and fish fats are usually unsaturated
  • Certain unsaturated fatty acids are not synthesized in the human body and must be supplied in the diet
    • Omega-3 fatty acids: required for normal growth and thought to provide protection against cardiovascular disease
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23
Q

Trans fat

A

An unsaturated fat, formed artificially during hydrogenation of oils, containing one or more trans double bonds.

  • Converts unsaturated fats to saturated fats by adding hydrogen.
  • Hydrogenating vegetable oils also creates unsaturated fats with trans double bonds
  • These trans fats may contribute more than saturated fats to cardiovascular disease
24
Q

Phospholipid

A
  • A lipid made up of glycerol joined to two fatty acids and a phosphate group.
  • The hydrocarbon chains of the fatty acids act as nonpolar, hydrophobic tails, while the rest of the molecule acts as a polar, hydrophilic head.
  • Phospholipids form bilayers that function as biological membranes.
    • When added to water, they self-assemble into a bilayer, with the hydrophobic tails pointing toward the interior. This results in a bilayer arrangement found in cell membranes
  • Phospholipids are the major component of all cell membranes
25
Q

Steroid

A

A type of lipid characterized by a carbon skeleton consisting of four fused rings with varius chemical groups attached.

26
Q

Cholesterol

A

A steroid that forms an essential component of animal cell mambranes and acts as a precursor molecule for the synthesis of other biologically important steroids, such as many hormones. High levels of cholesterol in the blood may contribute to cardiovascular disease.

27
Q

Protein

A
  • A biologically functional molecule consisting of one or more polypeptides folded and coiled into a specific three-dimensional structure.
  • Account for more than 50% of the dry mass of most cells
  • Functions include structural support, storage, transport, cellular communications, movement, and defense against foreign substances
  • The sequence of amino acids determines a protein’s three-dimensional structure
    • A protein’s structure determines its function
28
Q

Enzymatic Proteins

A
  • A macromolecule serving as a catalyst, a chemical agent that increases the rate of a reaction without being consumed by the reaction.
  • Can perform their functions repeatedly, functioning as workhorses that carry out the processes of life
29
Q

Storage Proteins

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30
Q

Hormonal Proteins

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31
Q

Contractile and Motor Proteins

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32
Q

Defensive Proteins

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33
Q

Transport Proteins

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34
Q

Receptor Proteins

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35
Q

Structural Proteins

A
36
Q

Polypeptides

A
  • A polymer of many amino acids linked together by peptide bonds.
  • Range in length from a few to more than a thousand monomers
  • Each polypeptide has a unique linear sequence of amino acids, with a carboxyl end (C-terminus) and an amino end (N-terminus)
37
Q

Amino Acid

A
  • An organic molecule possessing both a carboxyl and an amino group.
  • Serve as the monomers of polypeptides
  • Differ in their properties due to differing side chains, called R groups
  • Linked by peptide bonds
38
Q

Peptide Bond

A

The covalent bond between the carboxyl group on one amino acid and the amino group on another, formed by a dehydration reaction.

39
Q

Functional Protein

A

Consists of one or more polypeptides precisely twisted, folded, and coiled into a unique shape.

40
Q

Primary Protein Structure

A
  • A protein’s unique senquence of amino acids.
    • Like the order of letters in a long word
  • Determined by inherited genetic information
  • A slight change in primary structure can affect a protein’s structure and ability to function
    • Sickle-cell disease, an inherited blood disorder, results from a single amino acid substitution in the protein hemoglobin
41
Q

Secondary Protein Structure

A
  • Found in most proteins
  • Consists of coils and folds in the polypeptide chain
    • These coils and colds of secondary structure result from hydrogen bonds between repeating constituents of the polypeptide backbone
  • Typical secondary structures are a coil called an α helix and a folded structure called a β pleated sheat
42
Q

Tertiary Protein Structure

A
  • Determined by interactions among various side chains (R groups), rather than interactions between backbone constituents
  • These interactions between R groups include hydrogen bonds, ionic bonds, hydrophobic interactions, and van der Waals interactions
43
Q

Quaternary Protein Structure

A

Results when a protein consists of myltiple polypeptide chains

  • Collagen is a fibrous protein consisting of three polypeptides coiled like a rope
  • Hemoglobin is a glubular protein consisting of four polypeptides: two alpha and two beta chains
44
Q

Disulfide Bridge

A

A strong covalent bond formed when the sulfur of one cysteine monomer bonds to the sulfur of another cysteine monomer.

  • May reinforce a protein’s structure
45
Q

Denaturation

A
  • In proteins, a process in which a protein loses its native shape due to the disruption of weak chemical bonds and interactions, thereby becoming biologically inactive
  • In DNA, the separation of the two strands of the double helix
  • Occurs under extreme conditions of pH, salt concentration, or temperature
    • A denatured protein is biologically inactive
46
Q

Chaperonins

A
  • Protein molecules that assist the proper folding of other proteins
    • Diseases such as Alzheimer’s, Parkinson’s, and mad cow diease are associated with misfolded proteins
47
Q

X-Ray Crystallography

A

A technique used to study the three-dimensional structure of molecules. It depends on the diffraction of an X-ray beam by the individual atoms of a crystallized molecule.

48
Q

Gene

A
  • A discrete unit of hereditary information consisting of a specific nucleotide sequence in DNA or RNA
  • The amino acid sequence of a polypeptide is programmed by genes
49
Q

Nucleic Acid

A
  • A polymer (polynucleotide) consisting of many nucleotide monomers
  • Serves as a blueprint for proteins and, through the actions of proteins, for all cellular activities
  • The two types are DNA and RNA
50
Q

Deoxyribonucleic Acid (DNA)

A
  • A nucleic acid molecule, usually a double-stranded helix, in which each polynucleotide strand consists of nucleotide monomers with a deoxyribose sugar and the nitrogenous bases adenine (A), cytosine (C), guanine (G), and thymine (T)
    • The nitrogenous bases in DNA pair up and form hydrogen bonds. Called complementary base pairing.
      • Adenine is always with thymine
      • Guanine is always with cytosine
  • Capable of being replicated and determining the inherited structure of a cell’s proteins.
  • Directs synthesis of messenger RNA (mRNA) and, through mRNA, controls protein synthesis
    • Protein synthesis occurs on ribosomes
  • In the DNA double helix, the two backbones run in opposite 5’ to 3’ directions from each other, an arrangement referred to as antiparallel
  • One DNA molecule includes many genes.
51
Q

Ribonucleic Acid (RNA)

A
  • A type of nucleic acid consisting of a polynucleotide made up of nucleotide monomers with a ribose sugar and the nitrogenous bases adenine (A), cytosine (C), guanine (G), and uracil (U)
  • Single polypeptide chain
  • functions in protein synthesis, gene regulation, and as the genome of some viruses
  • Complementary pairing is similar to DNA
    • Thymine is replaced by uracil so adenine and uracil pair
52
Q

Polynucleotide

A
  • A polymer consisting of many nucleotide monomers in a chain. The nucleotides can be those of DNA or RNA.
  • Adjacent nucleotides are joined by covalent bonds that form between the -OH group on the 3’ carbon of one nucleotide and the phosphate on the 5’ carbon on the next
    • These links create a backbone of sugar-phosphate units with nitrogenous bases as appendages
53
Q

Nucleotide

A
  • The building block of a nucleic acid, consisting of a five-carbon sugar covalently bonded to a nitrogenous base and one or more phosphate groups
  • Nucleotide = Nucleoside + phosphate group
  • The portion of a nucleotide without the phosphate group is called a nucleoside
    • Nucleoside = Nitrogenous base + sugar
54
Q

Pyrimidine

A
  • One of the two types of nitrogenous bases found in nucleotides, characterized by a six-membered ring.
  • Cyosine (C), thymine (T), and uracil (U) are pyrimidines
55
Q

Purine

A
  • One of the two types of nitrogenous bases found in nucleotides, characterized by a six-membered ring fused to a five-membered ring.
  • Adenine (A) and guanine (G) are purines.
56
Q
A