BIOL 1406 Chapter 05 Flashcards

1
Q

four classes of large biological molecules

A

carbohydrates, lipids, proteins, and nucleic acids

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2
Q

Macromolecules

A

are large molecules composed of thousands of covalently connected atoms

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3
Q

polymer

A

is a long molecule consisting of many similar building blocks

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4
Q

monomers

A

small building-block molecules

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5
Q

condensation / dehydration reaction

A

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

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6
Q

enzymes

A

macromolecules that speed up the dehydration process

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7
Q

hydrolysis

A

Polymers are disassembled to monomers by hydrolysis, a reaction that is essentially the reverse of the dehydration reaction

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8
Q

carbohydrates

A

include sugars and the polymers of sugars

The simplest carbohydrates are monosaccharides, or single sugars

Carbohydrate macromolecules are polysaccharides, polymers composed of many sugar building blocks

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9
Q

monosaccharides

A

have molecular formulas that are usually multiples of CH2O

Glucose (C6H12O6) is the most common monosaccharide

Monosaccharides are classified by the location of the carbonyl group (as aldose or ketose); the number of carbons in the carbon skeleton

Monosaccharides serve as a major fuel for cells and as raw material for building molecules

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10
Q

disaccharide

A

is formed when a dehydration reaction joins two monosaccharides. This covalent bond is called a glycosidic linkage.

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11
Q

polysaccharides

A

the polymers of sugars, have storage and structural roles. The structure and function of a polysaccharide are determined by its sugar monomers and the positions of glycosidic linkages.

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12
Q

starch

A

a storage polysaccharide of plants, consists entirely of glucose monomers

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13
Q

glycogen

A

is a storage polysaccharide in animals. Humans and other vertebrates store glycogen mainly in liver and muscle cells

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14
Q

cellulose

A

a polysaccharide, is a major component of the tough wall of plant cells

is a polymer of glucose, but the glycosidic linkages differ

The difference is based on two ring forms for glucose: alpha and beta

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15
Q

chitin

A

another structural polysaccharide, is found in the exoskeleton of arthropods.

Chitin also provides structural support for the cell walls of many fungi

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16
Q

lipids

A

are the one class of large biological molecules that do not form polymers.

The unifying feature of lipids is having little or no affinity for water.

Lipids are hydrophobic becausethey consist mostly of hydrocarbons, which form nonpolar covalent bonds.

The most biologically important lipids are fats, phospholipids, and steroids.

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17
Q

saturated fatty acids

A

have the maximum number of hydrogen atoms possible and no double bonds

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18
Q

unsaturated fatty acids

A

have one or more double bonds

19
Q

hydrogenation

A

is the process of converting unsaturated fats to saturated fats by adding hydrogen

20
Q

phospholipid

A

two fatty acids and a phosphate group are attached to glycerol. The two fatty acid tails are hydrophobic, but the phosphate group and its attachments form a hydrophilic head

21
Q

steroids

A

are lipids characterized by a carbon skeleton consisting of four fused rings

22
Q

cholesterol

A

an important steroid, is a component in animal cell membranes

23
Q

enzymatic proteins

A

function: selective acceleration of chemical reactions
example: digestive enzymes

24
Q

structural proteins

A

function: support
example: silk fibers, collagen and elastin in animal connective tissues; keratin in hair, horns, feathers

25
Q

storage proteins

A

function: storage of amino acids
example: ovalbumin in egg white; casein, the protein of milk; storage proteins in plant seeds

26
Q

transport proteins

A

function: transport of other substances
example: hemoglobin, transport proteins

27
Q

hormonal proteins

A

function: coordination of an organism’s activities
example: insulin, a hormone secreted by the pancreas

28
Q

receptor proteins

A

function: response of cell to chemical stimuli
example: receptors in nerve cell membranes

29
Q

contractile and motor proteins

A

function: movement
example: actin and myosin in muscles, protein in cilia and flagella

30
Q

defensive proteins

A

function: protection against disease
example: antibodies combat bacteria and viruses

31
Q

enzymes

A

are a type of protein that acts as a catalyst to speed up chemical reactions

32
Q

polypeptides

A

are polymers built from the same set of 20 amino acids

33
Q

protein

A

consists of one or more polypeptides

34
Q

amino acids

A

are organic molecules with carboxyl and amino groups.

Amino acids differ in their properties due to differing side chains, called R groups

linked by peptide bonds

35
Q

Four Levels of Protein Structure

A

The primary structure of a protein is its unique sequence of amino acids.
Secondary structure, found in most proteins, consists of coils and folds in the polypeptide chain.
Tertiary structure is determined by interactions among various side chains (R groups).
Quaternary structure results when a protein consists of multiple polypeptide chains.

36
Q

Primary Structure

A

the sequence of amino acids in a protein, is like the order of letters in a long word

Primary structure is determined by inherited genetic information

37
Q

Secondary Structure

A

The coils and folds of secondary structure result from hydrogen bonds between repeating constituents of the polypeptide backbone

Typical secondary structures are a coil called an  helix and a folded structure called a  pleated sheet

38
Q

Tertiary Structure

A

is determined by interactions between 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

Strong covalent bonds called disulfide bridges may reinforce the protein’s structure

39
Q

Quaternary Structure

A

results when two or more polypeptide chains form one macromolecule

Collagen is a fibrous protein consisting of three polypeptides coiled like a rope

Hemoglobin is a globular protein consisting of four polypeptides: two alpha and two beta chains

40
Q

denaturation

A

loss of a protein’s native structure

41
Q

chaperonins

A

are protein molecules that assist the proper folding of other proteins

42
Q

x-ray crystallography

A

to determine a protein’s structure

43
Q

nuclear magnetic resonance (NMR) spectroscopy

A

which does not require protein crystallization

44
Q

bioinformatics

A

uses computer programs to predict protein structure from amino acid sequences