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AP Tignor 1 > Chap 2 Chemistry And Biochem > Flashcards

Chap 2 Chemistry And Biochem Flashcards

1
Q

Biochemistry

A

Chemical composition and reactions of living things

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2
Q

Types of chemicals in the body

A

Organic
Inorganic

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3
Q

Organic compounds

A

Have carbon
Made by living things

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4
Q

Types of bonds in all organic compounds

A

Covalent
Usually large

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5
Q

Inorganic compounds

A

Don’t have carbon

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6
Q

Examples of inorganic compounds

A

Water, salts, acids, bases

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7
Q

Exceptions of inorganic compounds

A

CO2 & CO

Have carbon but considered inorganic

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8
Q

T o F Both organic and inorganic compounds are important?

A

True

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9
Q

Water makes up what volume of living things?

A

60-80%

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10
Q

Most abundant and important inorganic compound?

A

Water

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11
Q

What properties make water special?

A

1.High heat capacity
2.High heat vaporization
3. Polar solvent properties

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12
Q

Why is high heat capacity useful?

A

Prevents changes in temperature. Takes a lot of energy to change it’s temperature so it’s good at maintaining stable conditions.

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13
Q

Why is high heat of vaporization useful?

A

Takes a lot of energy for water to evaporate. Helps cool when sweat. Our body releases large amounts of energy to make sweat evaporate, cooling us off in the process

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14
Q

Why are polar solvent properties useful?

A

Biological molecules don’t react unless they’re in solution. All reactions in the body depend on water’s solvent properties. Good at attracting molecules and surrounding them

Can transport things

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15
Q

Hydration layers

A

Layers of water molecules around large charged molecules. Protects from other charged molecules & prevents them from settling out of solution.

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16
Q

Biological colloids

A

Protein water mixtures
Blood plasma
CSF

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17
Q

Importance of Reactivity in water

A

Water is an important chemical reactant in many reactions. Breaking down food molecules through hydrolysis

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18
Q

Importance of water’s cushioning

A

Not compressible but it can flow. Form cushions around organs. Protects from trauma. CSF

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19
Q

Salt

A

Ionic compound. Has cations other than H+
Anions other than OH-

Dissociates into components

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20
Q

Electrolytes

A

Substances that conduct electrical currents when in solution.
All ions

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21
Q

Examples of common salts in the body

A

NaCl,
CaCO3
KCl

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22
Q

Most plentiful salts in body

A

Calcium phosphates that make bones and teeth hard

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23
Q

What are salts good for?

A

Na &K ions important for muscle contractions
Fe ions make hemoglobin

Zn and Cu maintain enzyme activity

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24
Q

Are acids and bases electrolytes?

A

Yes they dissociate and can conduct electrical currents

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25
Q

Acids properties

A

Dissolve metals, sour taste. Releases H+ ions
Proton donor because H+ is only proton

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26
Q

What determines the acidity of a solution?

A

H+ concentration

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27
Q

What’s a good way to recognize the formula for an acid?

A

It will have an H in the beginning

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28
Q

Bases properties

A

Bitter taste, feel slippery, proton acceptors

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29
Q

Common inorganic bases

A

Hydroxides, dissolve in water but liberate OH- and cations

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30
Q

Bicarbonate ion importance

A

Important base in body, abundant in blood

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31
Q

What does Ammonia do?

A

Base.Common waste product of protein breakdown in body.
Attracts protons with it’s one pair of unshared electrons. Ammonia becomes ammonium

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32
Q

What do pH units measure?

A

Relative concentration of H ions in body fluids

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33
Q

Each change of pH represents a ____X change in H+ concentration

A

10

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34
Q

Formal definition of pH

A

Negative log of H+ concentration in Moles/Liter

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35
Q

When is a solution neutral

A

pH=pOH

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36
Q

life preserving enzymes in body work within narrow pH range. T or F

A

True

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37
Q

Buffers

A

Resist abrupt and large swings in pH of body fluids by releasing and binding H as needed

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38
Q

What are buffers made of ?

A

Weak acid, weak base

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39
Q

Explain the bicarbonate buffer system

A
  1. Carbonic acid dissociates into bicarbonate and a proton
  2. When blood pH lowers (more acidic) bicarbonate binds H+

when blood pH is higher carbonic acid releases H

Strong bases are turned to weak bases and protons are bound to make weak acids

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40
Q

Electroneutral

A

Never loses or gain electrons

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41
Q

Why is carbon’s electroneutrality important?

A

Makes 4 covalent bonds, can make long chains, never loses or gains electrons

Can make various different shapes

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42
Q

Macromolecules

A

Complex molecules containing thousands of atoms.

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43
Q

Which process binds monomers?

A

Dehydration synthesis

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44
Q

Explain dehydration synthesis

A
  1. A Hydrogen is removed from one monomer and a hydroxyl is removed from the monomer that it will be joined with. A water molecules is removed from the bond site each time more monomers bind
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45
Q

Hydrolysis

A

Molecules split using water

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46
Q

Functional groups

A

Parts of organic molecules where reactions occur.

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47
Q

What percentage of cell mass are carbs?

A

1-2%

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48
Q

Ratio of H and O in carbohydrates

A

2:1
Hydrated carbon

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49
Q

Ways to classify carbohydrates

A

Size and solubility

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50
Q

Classification by size

A

Monosaccharide
Disaccharides
Polysaccharides

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51
Q

What is more soluble in water monosaccharide or polysaccharide?

A

Monosaccharide..
Bigger molecules are less soluble

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52
Q

Monosaccharides

A

Single ring or single chain 3-7 carbon atoms

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53
Q

Ratio of monosaccharides and formula

A

1:2:1
(CH2O)n
n= number of carbons in the sugar

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54
Q

Which monosaccharides are most important in the body?

A

Pentose and hexose

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55
Q

Example of pentose

A

Deoxyribose

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56
Q

Example of hexose

A

Glucose

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57
Q

Isomers

A

Same formula, different arrangement so different chemical properties

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58
Q

Examples of isomers of glucose

A

Galactose
Fructose

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59
Q

Disaccharides

A

Double sugars
Formed by dehydration synthesis

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60
Q

Disaccharides

A

Sucrose
Lactose
Maltose

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61
Q

Sucrose

A

Glucose + fructose
Cane sugar

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62
Q

Can disaccharides go through cell membrane?

A

No must be hydrolysed to monosaccharides

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63
Q

Polysaccharides

A

Polymers of simple sugars
Storage

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64
Q

Important polysaccharides

A

Glycogen
Starch
(Polymers of glucose)

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65
Q

Starch

A

Storage carb made by plants

Found in grains and potatoes

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66
Q

Cellulose function

A

Not digested
Bulk of fiber

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67
Q

Glycogen stored in

A

Liver and skeletal muscle

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68
Q

How is glycogen used?

A

Muscles use it to move
Liver uses it to maintain blood sugar. Let’s body cells get fuel

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69
Q

Carbohydrates roles

A

Ready, easily used source of fuel
Most cells can only use simple sugars like glucose

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70
Q

Lipids dissolve in

A

Other lipids sand alcohol and ether

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71
Q

Amount of oxygen in lipids is higher or lower?

A

Lower

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72
Q

Triglycerides

A

Major form of stored energy in the body
Fat deposits in subcutaneous tissue and around organs. Protect and insulate organs.

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73
Q

Phospholipids

A

Chief part of cell membrane

Transport lipids in blood. Part of lipoproteins

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74
Q

Types of steroids

A

Cholesterol
Bile salts
Vitamin D
Sex hormones
Corticosteroids

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75
Q

Cholesterol

A

Component of all cell membranes

Starts synthesis of all body steroids

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76
Q

corticosteroids

A

cortisol
aldosterone

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77
Q

Bile salts

A

Made by breakdown of cholesterol,
released by liver into digestive tract to help with fat digestion and absorption.

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78
Q

Vitamin D

A

Made in skin after UV radiation touches skin
Needed for bone growth and function

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79
Q

Sex hormones

A

Estrogens and progesterone
made in gonads

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80
Q

cortisol

A

maintains glucose levels

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81
Q

Aldosterone

A

regulates salt and water balance, targeting kidneys

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82
Q

Fat soluble vitamins

A

ADEK

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83
Q

Eicosanoids

A

prostaglandins and thromboxanes

made from fatty acids found in all cell membranes

84
Q

Prostaglandins
functions

A

promote inflamation
stim. contractions
regulate BP
controlling GI movement
Blood clotting

85
Q

Thromboxanes

A

powerful vasoconstrictors

86
Q

Lipoproteins

A

Lipid and protein based substances, transport fatty acids and cholesterol in blood

Major kinds are High density and Low density

87
Q

Glycolipids

A

Parts of Cell membranes

Carbs attached to lipids determine blood type.

help cell recognition and recognition of foreign substances

88
Q

Triglycerides are known as ____ when solid

A

fats

89
Q

Triglycerides are known as ___ when liquid

A

oils

90
Q

Most efficient and compact form of stored energy?

A

Triglycerides

91
Q

When do triglycerides yield large amounts of energy?

A

When oxidized

92
Q

Building blocks of triglycerides?

A

Three fatty acids and a glycerol

93
Q

Fatty acids

A

Hydrocarbon chains that end with COOH

94
Q

Glycerol

A

modified simple sugar (sugar alcohol)

95
Q

Why do fats have to be broken down to absorb?

A

Oil and water don’t mix. Ingested fats and oils must be broken down to their building blocks. Polar and nonpolar don’t interact.

96
Q

Why are woman better english channel swimmers?

A

The fat helps insulate them from cold water

97
Q

Saturated fats

A

single covalent bonds
straight chains
solid at room temp because closely packed

98
Q

Unsaturated fats

A

one or more double bonds (mono or poly unsaturated)

kinked chains, can’t solidify.

More heart healthy

99
Q

Trans fats

A

oils that are solidified by adding H at carbon double bonds. Increase heart disease risk

100
Q

Omega 3 fatty acids benefits

A

Decrease risk of heart disease and inflammatory diseases

101
Q

Difference between phsopholipids and triglycerides

A

2 fatty acids and a phosphate

102
Q

Steroids structure

A

flat, four interlocking hydrocarbons. Fat soluble, little oxygen

103
Q

Most important molecule in steroid chemistry

A

Cholesterol

104
Q

Sources of cholesterol?

A

eggs, meat, cheese, liver

105
Q

Atherosclerosis

A

Fat buildup in walls of arteries

106
Q

NSAIDS

A

Non steroidal anti-inflammatory drugs, ibuprofen. Block actions of prostaglandins

107
Q

Percentage of proteins in cell mass?

A

10-30%

108
Q

basic structural material of body

A

proteins

109
Q

Structural proteins

A

mechanical support, example, collagen most abundant protein in body

110
Q

Enzyme proteins

A

needed for all biochemical reactions. disaccharidases hydrolyze disaccharides, proteases hydrolyze proteins. oxidase oxidizes food fuels

111
Q

transport proteins

A

move substances in blood or across membrane. Hemoglobin or transport proteins in cell membrane.

112
Q

Contractile proteins

A

movement
actin and myosin cause muscle contraction. help during cell division

113
Q

Communication proteins

A

transmitting signals between cells. Cheical messengers. Insulin

114
Q

Defensive proteins

A

protect against disease. Antibodies bind and inactivate foreign substances

115
Q

building blocks of proteins

A

aminoacids

116
Q

Parts of aminoacids

A

Amine group and acid group

117
Q

t/f amino acid can act as base or acid

A

true

118
Q

what makes aminoacids chemically unique?

A

R groups

119
Q

elements in aminoacids

A

CHON 2 have S

120
Q

How do aminoacids bind?

A

dehydration synthesis, the amine ends and amino acid groups are bound.

121
Q

peptide bond

A

joins aminoacids
binds carboxyl group to amine group. loss of h2o

122
Q

polypeptide

A

10 or more aminoacids bound

123
Q

how many common aminoacids?

A

20

124
Q

Primary structure of proteins

A

Amino acid chains. linear sequence of aminoacids

125
Q

secondary structure

A

alpha helices or beta pleated sheets

126
Q

tertiary structure

A

secondary structures are folded to globular form. Involves R groups on secondary structure are attracted to eachother

127
Q

quartenary structure

A

Two or more polypeptides with tertiary structure combine

128
Q

most common type of secondary structure

A

alpha helix. Stabilized by hydrogen bonds between NH ans CO. Link different parts of same chain together

129
Q

T/F Beta pleated sheetscan be made of different polypeptides

A

T?

130
Q

Transthyretin

A

transports thyroid hormone

131
Q

What determines the structure of a protein

A

its primary structure

132
Q

positions of hydrophillic and hydrophobic aminoacids in proteins

A

hydrophillic near surface, hydrophobic in core

133
Q

Most abundant protein in body

A

collagen

134
Q

characteristics of fibrous proteins

A

contractile some
insoluble in water

135
Q

Functional proteins characteristics

A

globular; compact sphereical, have at least tertiary structure, water soluble, chemically active. immunity, hormones, transport

136
Q

Are globular proteins stable or unstable?

A

unstable

137
Q

What causes hydrogen bonds to break?

A

low pH
High temp

138
Q

Denatured proteins

A

Proteins unfold because hydrogen bonds due to changes in pH or temperature

139
Q

irreversibly denatured

A

protein can’t go back to original form. Chaneg in conditions too extreme. Scrambled egg

140
Q

active sites

A

regions that fit and interact chemically with other complimentary molecules.

141
Q

How can enzymes be destroyed?

A

active site destroyed through denaturation because of extreme changes.

142
Q

Can enzymes force molecules to react?

A

NO

143
Q

apoenzyme

A

protein portion of an enzyme

144
Q

cofactor

A

metal ion or organic molecule needed for enzymatic activity

145
Q

holoenzyme

A

apoenzyme+cofactor

146
Q

Substrate

A

Substance an enzyme acts on

147
Q

catalytic activity happens at

A

active site

148
Q

are enzymes chemically specific?

A

yes, certian enzymes only bind to certain chemicals or certain groups of chemicals

149
Q

Do enzymes require activation?

A

some of them, this keeps enzymes from functioning where they’re not supposed to

150
Q

Activation energy

A

amount of energy needed for reaction to occur

151
Q

When do you need activation energy?

A

for all reactions, regardless of endergonic or exergonic

152
Q

How do enzymes speed up reactions?

A

By lowering the activation energy needed to function

153
Q

Explain the mechanism of enzyme activation

A

E+S-> E-S ->P+E

  1. active site changes shape to bind substrate
  2. ES complex rearrages internally to make products. then returns to original shape
  3. Enzyme can catalyze millions of times within a minute
154
Q

Enzyme inhibitor

A

subtance shaped like substrate blocks binding site

155
Q

Which example of protein structure involves interactions between the R-groups of distantly positioned amino acids along the polypeptide chain?

A

tertiary structure

156
Q

Which bonds within ATP are considered “high-energy”?

A

-phosphate -phosphate
bond between 2nd and third phosphate groups gives energy transferred to other molecules during cellular work

157
Q

largest molecules in the body?

A

nucleic acids DNA RNA

158
Q

DNA

A

in nucleus, genetic material, genome

159
Q

Roles of DNA

A

Replicates
Instructions for building every protein

160
Q

Major cellular site of RNA

A

Cytoplasm

161
Q

Major functions of RNA

A

genetic instructions for protein synthesis

162
Q

Structure of RNA

A

single strand, straight or folded

163
Q

sugar in RNA

A

ribose

164
Q

Bases in RNA

A

AG CU

165
Q

Major cellular site of DNA

A

Nucleus

166
Q

structure of DNA , sugar, bases

A

doublehelix, deoxyribose, AG CT

167
Q

uses of DNA

A

fingerprinting, paternity tests, crime identification of body

168
Q

molecular slave of DNA

A

RNA except for viruses where rna is the main genetic material

169
Q

Types of RNA

A

rRNA
tRNA
mRNA

170
Q

microRNA

A

Small RNA molecules

171
Q

nucleotides

A

structural units of nucleic acids

172
Q

Parts of a nucleotide

A

nitrogen containing base, pentose sugar
phosphate

173
Q

purines, larger double ringed

A

adenine and guanine

174
Q

Pyrimidines, smaller, single ring

A

Cytoside, thymine, uracil

175
Q

backbone of DNA

A

Alternating sugar and phospahtecomponents

176
Q

A bonds to

A

T

177
Q

G bonds to

A

C

178
Q

U replaces

A

T

179
Q

Primary energy transferring molecule

A

ATP

180
Q

Phosphorylation

A

Passing the P from ATP to another molecule

181
Q

Most important cellular fuel

A

Glucose

182
Q

Structure of ATP

A

RNA nucleotide with two more phosphates

183
Q

What lets ATP store energy?

A

3 negatively charged phosphate groups repel eachother

184
Q

What happens after phsphorylation?

A

Molecules more active, can perform cellular work. after they do the work they lose the phosphate. energy released by phosphate is close to activation energy. chemical work, mechanical work, transport work

185
Q

Acidosis

A

blood pH below 7.35

186
Q

Alkalosis

A

pH higher than 7.45.

187
Q

heavy metals toxic

A

arsenic, mercury, and lead. Iron, also included in this group, is toxic in high concentrations.

188
Q

ionizing radiation

A

causes atoms to ionize, gamma rays, xrays

189
Q

Radiation sickeness,

A

disease caused by radioactivity. Rapidly dividing cells are most affected. blood forming cells and digestive tract cells most affected

190
Q
A
191
Q

Make 90% of elements in body by mass

A

CHON

192
Q

Phosphorus

A

Calcium phosphate in bones

ATP

193
Q

Potassium

A

Dissolved electrolyte in blood plasma

194
Q

Sulfur

A

Protein folding

195
Q

Cystine

A

Make disulfur bridges to shape proteins

196
Q

Na

A

Electrolyte for depolarization to pass on potentials

197
Q

Trace elements

A

If it looks like a metal,
Help proteins fold like hemoglobin.

198
Q

For every proton there is

A

An electron

199
Q

Mass of protons and neutrons

A

1 amu

200
Q

Isotopes

A

Same number of protons , dif number of neutrons

201
Q

Kalemia

A

Potassium

202
Q

Iodine is used in

A

Hormones made by thyroid

203
Q

Which type of compound contains carbon and hydrogen?

A

Organic

204
Q

Atoms

A

Smallest part of an element. Has components like electrons, protons, neutrons

205
Q

Elements

A

Pure substance that cannot be broken down into simpler substances

206
Q

Molecules

A

2 or more atoms held together by chemical bonds

Same element

207
Q

Compound

A

Made by 2 or more different types of elements

AP Tignor 1 (29 decks)

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