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Anatomy & Physiology > 2 Organic Compounds > Flashcards

2 Organic Compounds Flashcards

1
Q

most organic molecules are very large; their interactions with other molecules involve what?

A

only small reactive parts of their structure called functional groups (acid groups, amines, others)

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2
Q

functional groups

A

the small reactive parts of an organic molecule’s structure

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3
Q

the small reactive parts of an organic molecule’s structure

A

functional groups

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4
Q

monomers

A

similar or repeating units

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5
Q

similar or repeating units

A

monomers

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6
Q

polymers

A

chainlike molecules made up of many similar or repeating units (monomers) which are joined together by dehydration synthesis

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7
Q

chainlike molecules made up of many similar or repeating units (monomers) which are joined together by dehydration synthesis

A

polymers

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8
Q

dehydration synthesis

A

process by which a larger molecule is made by smaller ones joining through the removal of a water molecule at each sit of bond formation; a covalent bond unites the monomers as a hydrogen is released by one and a hydroxyl group by the other

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9
Q

process by which a larger molecule is made by smaller ones joining through the removal of a water molecule at each sit of bond formation

A

dehydration synthesis

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10
Q

the reverse process of dehydration syntheses

A

hydrolysis

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11
Q

a water molecule is added to bonded monomers and the bond is broken, releasing the monomers and breaking down polymers

A

hydrolysis

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12
Q

hydrolysis

A

the process in which water is used to split a substance into smaller particles; a water molecule is added to bonded monomers to break the bond

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13
Q

other than the monomers, all organic molecules share this in common

A

they are formed by dehydration synthesis and broken down through hydrolysis

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14
Q

carbohydrate

A

organic compound composed of carbon hydrogen and oxygen (CHO). includes sugars, starches and cellulose

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15
Q

organic compound composed of carbon hydrogen and oxygen (CHO). includes sugars, starches and cellulose

A

carbohydrate

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16
Q

CHO

A

carbohydrate, carbon hydrogen oxygen

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17
Q

carbohydrate means “hydrated carbon” what does this mean?

A

in carbohydrates, the hydrogen and oxygen atoms appear in the same ratio as water so it is H2O plus carbon C6H12O6 or C5H10O5

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18
Q

what are the three classification of carbohydrates?

A

classified according to size and solubility in water:
monosaccharides
disaccharides
polysaccharides

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19
Q

what are the structural units, or building blocks, of carbohydrates and why?

A

monosaccharides, because they are joined to form the molecules of the other two carbohydrate groups

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20
Q

monosaccharides

A

means one sugar; referred to as simple sugars

single-chain or single-ring structures containing 3 to 7 carbon atoms

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21
Q

means one sugar; referred to as simple sugars

single-chain or single-ring structures containing 3 to 7 carbon atoms

A

monosaccharides

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22
Q

important monosaccharides in the body

A 
glucose
fructose
galactose
ribose
deoxyribose
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23
Q

what is blood sugar?

A

glucose

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24
Q

what is known as the universal cellular fuel?

A

glucose

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25
Q

what monosaccharides are converted to glucose for use by body cells?

A

fructose and galactose

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26
Q

what monosaccharides form part of the structure of nucleic acids?

A

ribose and deoxyribose

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27
Q

disaccharides

A

means double sugars, are formed when two simple sugars (monosaccharides) are joined by dehydration synthesis

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28
Q

means double sugars, are formed when two simple sugars are joined by dehydration synthesis

A

disaccharides

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29
Q

important disaccharides in the diet

A

sucrose (glucose-fructose); cane sugar
lactose (glucose-galactose); found in milk
maltose (glucose-glucose0; malt sugar

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30
Q

C6H12O6

A

glucose

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31
Q

what must happen for disaccharides to be absorbed from the digestive tract into the blood and why?

A

double sugars are too large to pass through cell membranes so they must be broken down (digested through hydrolysis) to their monosaccharide units to be absorbed from the digestive tract into the blood

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32
Q

long branching chains of linked simple sugars

A

polysaccharides; “many sugars”

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33
Q

what are polysaccharides useful for and why?

A

they are large, insoluble molecules which make them ideal storage products

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34
Q

besides their large size, how are polysaccharides different from disaccharides?

A

because of their large size they lack the sweetness of the simple and double sugars

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35
Q

important polysaccharides in the body

A

starch and glycogen

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36
Q

starch

A

the storage polysaccharide formed by plants

we ingest it in the form of “starchy” foods like grain and root vegetables

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37
Q

the storage polysaccharide formed by plants

we ingest it in the form of foods like grain and root vegetables

A

starch

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38
Q

glycogen

A

is a slightly smaller polysaccharide than starch but similar, it is found in animal tissues (mostly muscles and liver) formed of linked glucose units

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39
Q

what provides a ready, easily used source of food energy for cells?

A

carbohydrates

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40
Q

what is the principle carbohydrate used for food and energy for the cells?

A

glucose

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41
Q

what happens when glucose is oxidized (combined with oxygen) in a complex set of chemical reactions?

A

it is broken down into carbon dioxide and water. some of the energy released as the bonds are broken is trapped in the bonds of ATP molecules

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42
Q

the energy currency for all body cells

A

ATP

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43
Q

what happens to dietary carbohydrates if they are not immediately needed for ATP synthesis?

A

they are converted to glycogen or fat and stored

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44
Q

what is used for structural purposes and represent 1 to 2 percent of cell mass?

A

carbohydrates

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45
Q

besides being a source of energy, where else are carbohydrates found?

A

small amounts used for structural purpose, represent 1 to 2 percent of cell mass
some sugars found in our genes
sugars are attached to outer surface of cell membranes where they act as road signs to guide cellular interactions

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46
Q

carbohydrates are ingested as what?

A

sugars and starches

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47
Q

how are carbohydrates and lipids alike structurally?

A

both contain CHO and are degraded by hydrolysis and built by dehydration synthesis

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48
Q

in what form do lipids enter the body?

A

fat-marbled meats, egg yolks, milk products and oils

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49
Q

the most abundant lipids in the body

A

triglycerides
phospholipids
steroids

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50
Q

how are lipids structurally different from carbohydrates?

A

both are made up of CHO but where carbohydrate’s keep the H and O ratio the same as water (H2O), in lipids the Carbon and Hydrogen atoms far outnumber the Oxygen atoms

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51
Q

can you dissolve lipids?

A

most lipids are insoluble in water but easily dissolve in other lipids and in organic solvents like alcohol and acetone

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52
Q

neutral fats

A

triglycerides

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53
Q

the building blocks of triglycerides

A

glycerol and fatty acids

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54
Q

molecule whose E shape resembles the tines of a fork

A

triglyceride

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55
Q

triglyceride

A

glycerol with three fatty acid chains attached. the result of their synthesis is an E-shaped molecule that resembles the tines of a fork

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56
Q

how are there different kinds of neutral fats?

A

the glycerol backbone is the same in all neutral fats (triglycerides) but the fatty acid chains vary, resulting in different kinds of neutral fats

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57
Q

what determines how solid a triglyceride molecule is at any given temperature?

A

the length of the triglyceride’s fatty acid chains and their type of C-C bonds

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58
Q

triglycerides having fatty acid chains with only single covalent bonds between carbon atoms

A

saturated fat

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59
Q

saturated fat

A

triglycerides having fatty acid chains with only single covalent bonds between carbon atoms
fatty acid chains are straight; solid at room temperature

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60
Q

fatty acid chains are straight

A

saturated fat

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61
Q

solid at room temperature

A

saturated fat

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62
Q

why is saturated fat solid at room temperature?

A

their fatty acid chains are straight and, at room temperature the molecules pack closely together

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63
Q

their fatty acid chains are straight and, at room temperature the molecules pack closely together

A

saturated fat

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64
Q

fatty acid chains pack closely together

A

saturated fat

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65
Q

fatty acids that contain one or more double bonds between carbon atoms

A

unsaturated

monounsaturated and polyunsaturated

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66
Q

what causes fatty acid chains to kink?

A

the double and triple bonds between carbon atoms

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67
Q

fatty acids that cannot pack closely enough to solidify

A

unsaturated fat

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68
Q

liquid at room temperature

A

unsaturated fat

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69
Q

unsaturated fat

A

monounsaturated and polyunsaturated
fatty acids that contain one or more double bonds between carbon atoms
fatty acid chains are kinked;
liquid at room temperature

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70
Q

triglycerides with short fatty acid chains or unsaturated fatty acids

A

oils (liquid at room temperature)

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71
Q

olive oil, soybean oil and safflower oil are examples of what kind of fat?

A

unsaturated

olive oil is monounsaturated and the others polyunsaturated

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72
Q

animal fats like butterfat and meat fat are examples of what kind of fat?

A

saturated

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73
Q

trans fats

A

oils that have been solidified by the addition of hydrogen atoms at the sites of the double-carbon bonds

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74
Q

oils that have been solidified by the addition of hydrogen atoms at the sites of the double-carbon bonds

A

trans fats

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75
Q

type of fat that increases the risk of heart disease even more than solid animal fat

A

trans fats

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76
Q

omega-3 fatty acids

A

found naturally in cold-water fish; decrease risk of heart disease and some inflammatory diseases

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77
Q

represent the body’s most abundant and concentrated source of usable energy

A

triglycerides, neutral fats

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78
Q

when they are oxidized, they yield large amounts of energy

A

triglycerides

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79
Q

stored chiefly in fat deposits beneath the skin and around body organs

A

triglycerides, neutral fats

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80
Q

where are triglycerides chiefly stored?

A

in fat deposits beneath the skin and around body organs

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81
Q

help insulate the body and protect deeper body tissues from heat loss and bumps

A

triglycerides stored in fat deposits

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82
Q

similar to triglycerides

A

phospholipids

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83
Q

difference in structure between phospholipids and triglycerides

A

phospholipids have a phosphorus-containing group instead of one of the fatty acid chains

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84
Q

structure of phospholipid

A

glycerol backbone, 2 fatty acid chains and phosphorus containing group which is the polar “head”

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85
Q

what gives phospholipids special chemical properties and polarity?

A

the phosphorus-containing “head” bears an electrical charge

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86
Q

structure is basically flat molecules formed of four interlocking rings

A

steroid

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87
Q

steroid

A

structure is basically flat molecules formed of four interlocking rings

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88
Q

compare steroids to fats

A

structures are different but both are mad largely of hydrogen and carbon atoms and are fat soluble

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89
Q

single most important steroid molecule

A

cholesterol

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90
Q

where do we get cholesterol from

A

ingest animal products like meat egg and cheese; some is made by liver regardless of diet

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91
Q

where is cholesterol found?

A

in cell membranes

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92
Q

what is the raw material of vitamin D, steroid hormones and bile salts?

A

cholesterol

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93
Q

cholesterol

A

single most important steroid molecule

raw material of vitamin D, steroid hormones and bile salt

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94
Q

what are the building blocks of lipids?

A

glycerol and fatty acids

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95
Q

what are the building blocks of carbohydrates?

A

monosaccharides

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96
Q

which type of lipid is abundant in cellular membranes?

A

phospholipids

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97
Q

salts are electrolytes. what does that mean?

A

they conduct an electrical current when dissolved in water

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98
Q

how do ionic bonds differ from covalent bonds?

A

ionic bonds electrons completely transferred

covalent bonds electrons are shared

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99
Q

what accounts for over 50% of the organic matter in the body and have the most varied functions of the organic molecules?

A

proteins

100
Q

how is protein like carbohydrates and lipids?

A

all contain carbon, oxygen, & hydrogen

101
Q

what elements are proteins made up of?

A 
Carbon
Oxygen
Hydrogen
Nitrogen
sometimes Sulfur
102
Q

the building blocks of proteins

A

amino acids which are small molecules

103
Q

what structure do all amino acid groups have?

A

an amine group (NH2) - gives basic properties

and acid group (COOH - allows them to act as acids

104
Q

all amino acids are identical except for what?

A

a single group of atoms called their R-group

105
Q

what makes each amino acid chemically and functionally unique?

A

differences in the R-group

106
Q

structure of protein

A

amino acids are joined together in chains to form large complex protein molecules containing 50-thousands of amino acids

107
Q

amino acid chains containing fewer than 50 amino acids

A

polypeptides

108
Q

amino acid chains containing more than 50 amino acids

A

proteins

109
Q

how do amino acids produce dfferent proteins?

A

the sequence in which the amino acids are bound together (each of the 20 amino acids are like a letter forming into “words” ie proteins)

110
Q

how many different amino acids are there?

A

20

111
Q

the four structural levels of protein

A

primary structure
secondary structure
tertiary structure
quaternary structure

112
Q

the primary structure of a protein

A

the sequence of amino acids composing the polypeptide chain; resembles a strand of amino acid “beads;” is the back bone of the protein molecule

113
Q

the sequence of amino acids composing the polypeptide chain

A

the primary structure of a protein

114
Q

resembles a strand of amino acid “beads”

A

the primary structure of a protein

115
Q

is the backbone of the protein molecule

A

the primary structure of protein

116
Q

secondary structural level of a protein

A

the amino acid chain twisting and bending upon itself to form a more complex structure

117
Q

the amino acid chain twisting and bending upon itself to form a more complex structure

A

the secondary structural level of a protein

118
Q

two types of secondary structural levels of proteins

A

alpha-helix (slinky)

beta-pleated sheet (accordion)

119
Q

the most common secondary structure of protein

A

alpha-helix

120
Q

alpha-helix

A

the most common secondary structure of protein; resembles a slinky or telephone cord coil; formed by coiling the primary chain and stabilized by hydrogen bonds; the hydrogen bonds always link different parts of the SAME chain together

121
Q

secondary structure of protein that resembles a slinky or telephone cord

A

alpha-helix

122
Q

secondary structure of protein formed by coiling the primary chain and stabilized by hydrogen bonds

A

alpha-helix

123
Q

secondary structure of protein that’s hydrogen bonds always link different parts of the SAME chain together

A

alpha-helix

124
Q

in this type of secondary structure of protein, the primary polypeptide chains do not coil, but are linked side by side by hydrogen bonds to form pleated, ribbon-like structures that resemble and accordion

A

beta-pleated sheet

125
Q

beta-pleated sheet

A

a secondary structure of protein; resembles an accordion; primary polypeptide chains are linked side by side by hydrogen bonds to form a pleated ribbon-like structure; hydrogen bonds can link together DIFFERENT polypeptide chains as well as different parts of the SAME chain that has folded back on itself

126
Q

secondary structure of protein that’s hydrogen bonds link together different polypeptide chains as well as different parts of the same chain that has folded back on itself

A

beta-pleated sheet

127
Q

tertiary structure of a protein

A

the three-dimensional shape of the polypeptide or protein; is achieved when alpha-helix or beta-pleated regions fold upon one another to produce a compact, ball-like (globular) molecule; unique structure; maintained by covalent and hydrogen bonds between amino acids that are often far apart on primary chain

128
Q

the three-dimensional shape of the polypeptide or protein

A

tertiary structure of a protein

129
Q

is achieved when alpha-helix or beta-pleated regions fold upon one another to produce a compact, ball-like (globular) molecule

A

tertiary structure of a protein

130
Q

unique structure; maintained by covalent and hydrogen bonds between amino acids that are often far apart on primary chain

A

tertiary structure of a protein

131
Q

quaternary structural level of protein

A

when TWO OR MORE polypeptide chains combine in a regular manner to form a complex protein

132
Q

the final structure of any protein (tertiary or quaternary) is very specific and is dictated by this

A

its primary structure; the types and positions of the amino acids in the protein backbone determines where bonds can form; hydrophobic and hydrophilic amino acids position near the protein’s core and surface

133
Q

based on their overall shape and structure, proteins are classified into these two proteins

A 
fibrous proteins (structural proteins)
globular proteins (functional proteins)
134
Q

another name for fibrous proteins

A

structural proteins

135
Q

another name for globular proteins

A

functional proteins

136
Q

fibrous proteins

A

appear most often in body structures; some only secondary structure but most tertiary & quaternary; very important in binding structures together and providing strength in certain tissue; also called structural proteins because they FORM STUCTURES

137
Q

collagen

A

fibrous protein; most abundant protein in body; found in bones, cartilage and tendons

138
Q

fibrous protein; most abundant protein in body; found in bones, cartilage and tendons

A

collagen

139
Q

keratin

A

fibrous protein; is the structural protein of hair and nails and the material that makes skin “tough”

140
Q

fibrous protein; is the structural protein of hair and nails and the material that makes skin “tough”

A

keratin

141
Q

globular proteins

A

mobile; generally compact, spherical molecules that have a tertiary or quaternary structure; water soluble; also called functional proteins because they DO THINGS; play crucial role in all biological processes

142
Q

appear most often in body structures; some only secondary structure but most tertiary & quaternary; very important in binding structures together and providing strength in certain tissue; also called structural proteins because they FORM STUCTURES

A

fibrous proteins

143
Q

mobile; generally compact, spherical molecules that have a tertiary or quaternary structure; water soluble; also called functional proteins because they DO THINGS; play crucial role in all biological processes

A

globular proteins

144
Q

antibodies

A

globular (functional) proteins; provide immunity; highly specialized proteins that recognize, bind with, and inactivate bacteria, toxins, and some viruses

145
Q

hormones

A

globular proteins; help regulate growth and development

146
Q

enzymes

A

globular (functional) proteins; biological catalysts; regulate essentially every chemical reaction in to body; hundreds of different ones very specific in their activities acting only specific molecules

147
Q

stability of the two kinds of proteins (fibrous and globular)

A

fibrous-exceptionally stable
globular-unstable; fragile hydrogen bonds are critical to maintaining their structure; easily broken by heat and excess pH

148
Q

denatured proteins

A

when a the three-dimensional structure of protein is destroyed by heat or excess pH; can no longer perform their physiological roles because their function depends on their structure

149
Q

when a the three-dimensional structure of protein is destroyed by heat or excess pH; can no longer perform their physiological roles because their function depends on their structure

A

denatured proteins

150
Q

active sites on a protein’s surface

A

particular collection of atoms that “fit” and interact chemically with other molecules of complementary shape and size; don’t “fit” if denatured

151
Q

particular collection of atoms on a protein’s surface that “fit” and interact chemically with other molecules of complementary shape and size; don’t “fit” if denatured

A

active sites

152
Q

catalyst

A

a substance that increase the rate of a chemical reaction without becoming part of the product or changed itself

153
Q

a substance that increase the rate of a chemical reaction without becoming part of the product or changed itself

A

catalyst

154
Q

how do enzymes act as catalysts?

A

they bind to and “hold” the reacting molecules (substrates) in the proper position for chemical interaction; once reaction has occurred, enzyme releases the product and is reusable

155
Q

what would happen without enzymes?

A

biochemical reaction would be too slow to sustain life

156
Q

globular (functional) proteins; provide immunity; highly specialized proteins that recognize, bind with, and inactivate bacteria, toxins, and some viruses

A

antibodies

157
Q

transport proteins

A

globular (functional) protein; transports oxygen in the blood (hemoglobin); others carry iron, cholesterol or other substances in the blood

158
Q

globular (functional) protein; transports oxygen in the blood (hemoglobin); others carry iron, cholesterol or other substances in the blood

A

transport proteins

159
Q

globular (functional) proteins; biological catalysts; regulate essentially every chemical reaction in to body; hundreds of different ones very specific in their activities acting only specific molecules

A

enzymes

160
Q

hydrolases

A

enzymes which add water

161
Q

enzymes which add water

A

hydrolases

162
Q

oxidases

A

enzymes which cause oxidation

163
Q

enzymes which cause oxidation

A

oxidases

164
Q

how can you recognize an enzyme by its name?

A

by the suffix -ase forming part of its name

165
Q

function of enzymes in blood clotting

A

uses both enzymes that are produced in inactive form and must be activated as well as enzymes that must be inactivated immediately after they have performed their function; blood vessel damaged; enzyme activated to clot blood then inactivated to stop clotting when enough

166
Q

Oxygen in the body

A

a major component of both organic and inorganic molecules; as a gas, essential to the oxidation of glucose and other food fuels, during which cellular energy (ATP) is produced

167
Q

Carbon in the body

A

the primary element in all organic molecules, including carbohydrates, lipids, proteins, and nucleic acids

168
Q

Hydrogen in the body

A

a component of most organic molecules; as an ion, it influences the pH of body fluids

169
Q

Nitrogen in the body

A

a component of proteins and nucleic acids (genetic material)

170
Q

Calcium in the body

A

found as a salt in bones and teeth; in ionic form, required for muscle contraction, neural transmission, and blood clotting

171
Q

Phosphorous in the body

A

present as a salt, in combination with calcium, in bones and teeth; also present in nucleic acids and many proteins; forms part of ATP

172
Q

Potassium in the body

A

in its ionic form, the major intracellular cation; necessary for the conduction of nerve impulses and for muscle contraction

173
Q

Sulfur in the body

A

a component of proteins (particularly contractile proteins of muscle)

174
Q

Sodium in the body

A

as an ion, the major extracellular cation; important for water balance, conduction of nerve impulses, and muscle contraction

175
Q

Chlorine in the body

A

in ionic (chloride) form, the most abundant extracellular ion

176
Q

Magnesium in the body

A

present in bone; also important cofactor for enzyme activity in a number of metabolic reactions

177
Q

Iodine in the body

A

needed to make functional thyroid hormones

178
Q

Iron in the body

A

a component of the functional hemoglobin molecule (which transports oxygen within red blood cells) and some enzymes

179
Q

a major component of both organic and inorganic molecules; as a gas, essential to the oxidation of glucose and other food fuels, during which cellular energy (ATP) is produced

A

Oxygen

180
Q

the primary element in all organic molecules, including carbohydrates, lipids, proteins, and nucleic acids

A

Carbon

181
Q

a component of most organic molecules; as an ion, it influences the pH of body fluids

A

Hydrogen

182
Q

a component of proteins and nucleic acids (genetic material)

A

Nitrogen

183
Q

found as a salt in bones and teeth; in ionic form, required for muscle contraction, neural transmission, and blood clotting

A

Calcium

184
Q

present as a salt, in combination with calcium, in bones and teeth; also present in nucleic acids and many proteins; forms part of ATP

A

Phosphorus

185
Q

in its ionic form, the major intracellular cation; necessary for the conduction of nerve impulses and for muscle contraction

A

Potassium

186
Q

a component of proteins (particularly contractile proteins of muscle)

A

Sulfur

187
Q

as an ion, the major extracellular cation; important for water balance, conduction of nerve impulses, and muscle contraction

A

Sodium

188
Q

in ionic form, the most abundant extracellular ion

A

Chlorine (chloride in ionic form)

189
Q

present in bone; also important cofactor for enzyme activity in a number of metabolic reactions

A

Magnesium

190
Q

needed to make functional thyroid hormones

A

Iodine

191
Q

a component of the functional hemoglobin molecule (which transports oxygen within red blood cells) and some enzymes

A

Iron

192
Q

Factors increasing the rate of chemical reactions

A

increased temperature
increased concentration of reacting particles
decrease in particle size
presence of catalysts

193
Q

Neutral fats (triglycerides) in the body

A

found in fat deposits (subcutaneous tissue and around organs); protect and insulate the body organs; the major source of stored energy in the body

194
Q

Phospholipids (cephalin and others)

A

found in cell membranes; participate in the transport of lipids in plasma; abundant in the brain and nervous tissue in general, where they help to form insulating white matter

195
Q

5 major steroids in body

A 
Cholesterol
Bile salts
Vitamin D
Sex hormones
Corticosteroids (adrenal cortical hormones)
196
Q

Cholesterol in the body

A

the basis of all steroids

197
Q

Bile salts in the body

A

a breakdown product of cholesterol; released by the liver into the digestive tract, where they aid in fat digestion and absorption

198
Q

Vitamin D in the body

A

a fat-soluble vitamin produced in the skin on exposure to UV radiation; necessary for normal bone growth and function

199
Q

Sex hormones in the body

A

estrogen and progesterone (female) and testosterone (male) produced from cholesterol; necessary for normal reproductive function; deficits result in sterility

200
Q

Corticosteroids (adrenal cortical hormones) in the body

A

cortisol, a glucocorticoid, is a long-term anti-stress hormone that is necessary for life; aldosterone helps regulate salt and water balance in body fluids by targeting the kidneys

201
Q

Vitamin A in the body

A

a fat-soluble vitamin; found in orange-pigmented vegetables (carrots) and fruits (tomatoes); part of the photoreceptor pigment involved in vision

202
Q

Vitamin E in the body

A

a fat-soluble vitamin; taken via plant product like wheat germ and green leafy vegetables; may promote wound healing and contribute to fertility, but not proven in humans; an antioxidant; may help to neutralize free radicals

203
Q

Vitamin K in the body

A

a fat-soluble vitamin; made available largely by the action of intestinal bacterial; also prevalent in a wide variety of foods; necessary for proper clotting of blood

204
Q

Prostaglandins in the body

A

derivatives of fatty acids found in cell membranes; various functions depending on the specific class, including stimulation of uterine contractions (inducing labor and abortions), regulation of blood pressure, and control of motility of the gastrointestinal tract; involved in inflammation

205
Q

Lipoproteins in the body

A

lipoid and protein-based substances that transport fatty acids and cholesterol in the bloodstream

206
Q

found in fat deposits (subcutaneous tissue and around organs); protect and insulate the body organs; the major source of stored energy in the body

A

neutral fats (triglycerides)

207
Q

found in cell membranes; participate in the transport of lipids in plasma; abundant in the brain and nervous tissue in general, where they help to form insulating white matter

A

Phospholipids

208
Q

the basis of all steroids

A

Cholesterol

209
Q

a breakdown product of cholesterol; released by the liver into the digestive tract, where they aid in fat digestion and absorption

A

Bile salts

210
Q

a fat-soluble vitamin produced in the skin on exposure to UV radiation; necessary for normal bone growth and function

A

Vitamin D

211
Q

estrogen and progesterone (female) and testosterone (male) produced from cholesterol; necessary for normal reproductive function; deficits result in sterility

A

Sex hormones

212
Q

cortisol, a glucocorticoid, is a long-term anti-stress hormone that is necessary for life; aldosterone helps regulate salt and water balance in body fluids by targeting the kidneys

A

Corticosteroids

213
Q

a fat-soluble vitamin; found in orange-pigmented vegetables (carrots) and fruits (tomatoes); part of the photoreceptor pigment involved in vision

A

Vitamin A

214
Q

a fat-soluble vitamin; taken via plant product like wheat germ and green leafy vegetables; may promote wound healing and contribute to fertility, but not proven in humans; an antioxidant; may help to neutralize free radicals

A

Vitamin E

215
Q

a fat-soluble vitamin; made available largely by the action of intestinal bacterial; also prevalent in a wide variety of foods; necessary for proper clotting of blood

A

Vitamin K

216
Q

derivatives of fatty acids found in cell membranes; various functions depending on the specific class, including stimulation of uterine contractions (inducing labor and abortions), regulation of blood pressure, and control of motility of the gastrointestinal tract; involved in inflammation

A

Prostaglandins

217
Q

lipoid and protein-based substances that transport fatty acids and cholesterol in the bloodstream

A

Lipoproteins

218
Q

the role of nucleic acids

A

they make up genes, the blueprint for life; dictate protein structure

219
Q

they make up genes, the blueprint for life

A

nucleic acids

220
Q

they dictate protein structure

A

nucleic acids

221
Q

what elements are nucleic acids composed of?

A 
Carbon
Oxygen
Hydrogen
Nitrogen
Phosphorus
222
Q

largest biological molecules in the body

A

nucleic acids

223
Q

building blocks of nucleic acids

A

nucleotides

224
Q

nucleotides’ 3 basic parts

A

a nitrogen-containing base (ATCGU)
a pentose (5-carbon) sugar
a phosphate group

225
Q

the five varieties of nucleotide bases

A 
Adenine  (A)
Guanine (G)
Cytosine (C)
Thymine (T)
Uracil      (U)
226
Q

the structural differences of the five nucleotide bases

A

A and G are large, two-ring bases, whereas the others are smaller, single-ring structures

227
Q

the two major kinds of nucleic acid

A 
deoxyribonucleic acid (DNA)
ribonucleic acid (RNA)
228
Q

how are the “backbones” and “rungs” of DNA formed?

A

the backbones are formed by alternating sugar and phosphate molecules; the rungs are formed by complementary bases (A to T, C to G) bound by hydrogen bonds

229
Q

DNA

A

genetic material found within the cell nucleus;
two roles: replicates itself exactly before the cell divides ensuring genetic info in every cell is identical; provides the instructions for building every protein in the body

230
Q

RNA

A

located outside the nucleus; can be considered “molecular slave” of DNA–carries out orders for protein synthesis issued by DNA

231
Q

structural difference of RNA compared to DNA

A

both formed together by joining nucleotides; RNA single stranded; U replaces T in pairing with A; its sugar is ribose instead of deoxyribose

232
Q

three major varieties of RNA

A

messenger RNA
ribosomal RNA
transfer RNA
each has specific role all to do with carrying out DNA’s instructions for building protein

233
Q

messenger RNA

A

carries the information for building the protein from the DNA genes to the ribosomes, the protein-synthesizing sites

234
Q

carries the information for building the protein from the DNA genes to the ribosomes, the protein-synthesizing sites

A

messenger RNA

235
Q

transfer RNA

A

ferries amino acids to the ribosomes for protein synthesis

236
Q

ferries amino acids to the ribosomes for protein synthesis

A

transfer RNA

237
Q

ribosomal RNA

A

forms part of the ribosomes, where it oversees the translation of the message and the binding together of amino acids to form proteins

238
Q

forms part of the ribosomes, where it oversees the translation of the message and the binding together of amino acids to form proteins

A

ribosomal RNA

239
Q

ATP

A

adenosine triphosphate; provides a chemical form of energy that all body cells can use

240
Q

ATP structurally

A

a modified nucleotide; consists of an adenine base, ribose sugar, and three phosphate groups; the phosphate groups are attached by high-energy phosphate bonds which are broken by hydrolysis to release energy

241
Q

a modified nucleotide; consists of an adenine base, ribose sugar, and three phosphate groups

A

ATP

242
Q

the phosphate groups of this molecule are attached by high-energy phosphate bonds which are broken by hydrolysis to release energy

A

ATP

243
Q

chemical equation of ATP releasing energy

A

ATP–> ADP + P + E

P=inorganic phosphate E=energy

244
Q

how is ATP replenished?

A

by the oxidation of food fuels; the same amount of energy must be captured and used to reattach the phosphate group to ADP to make ATP

245
Q

ATP–>ADP–>ATP–>ADP–what is the process

A

the high-energy phosphate bonds are being attached and broken; when the phosphate group is attached & energy is stored it is ATP, broken off & energy released it is ADP

246
Q

how do glucose and ATP work together to provide energy?

A

glucose is the most important fuel for body cells but none of the chemical energy contained in its bonds can be used directly. Energy is released as glucose is catabolized and is captured & stored in the bonds of ATP; glucose is the fuel, ATP is the fire

Anatomy & Physiology (13 decks)

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