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SPORT SCIENCE > BIOCHEMISTRY > Flashcards

BIOCHEMISTRY Flashcards

1
Q

define an atom

A

smallest unit of an element

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2
Q

what does an atom contain

A

nucleus (protons & neutrons)

electrons

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3
Q

what is within a nucleus

A

protons

neutrons

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4
Q

what charge are protons

A

positive

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5
Q

what charge are neutrons

A

neutral

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6
Q

what charge are electrons

A

negative

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7
Q

what is the atomic number

A

number of protons

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8
Q

what is atomic mass measured in

A

Daltons (Da)

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9
Q

what is atomic mass

A

gives us the mass of one of the elements atoms

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10
Q

how many elements known to make up living organisms

A

26

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11
Q

what is covalent bonding

A

the bond formed when atoms share electrons

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12
Q

when is a single bond formed

A

when each atom contributes one electron

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13
Q

when is a double bond formed

A

when each atom contributes 2 electrons

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14
Q

what do organic molecules contain

A

carbon

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15
Q

what do inorganic molecules contain

A

NO CARBON (eg water)

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16
Q

what is a molecule

A

atoms joined via covalent bonds

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17
Q

what is molecular formula

A

symbols

eg H20

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18
Q

what is structural formula

A

drawn out with C and H and lines

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19
Q

do molecules have a charge

A

no they are neutral

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20
Q

do ions have charge

A

yes

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21
Q

what is an anion

A

some atoms are more stable with more electrons than protons

therefore ion carries a negative charge

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22
Q

what is a cation

A

some atoms carry less electrons than protons

therefore ion carries a positive charge

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23
Q

what is a radical

A

when a molecule has an unpaired electron

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24
Q

what pH is acidic

A

1-7

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25
Q

what pH is neutral

A

7

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26
Q

What pH is alkaline

A

7-14

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27
Q

what are the 4 biomolecules

A

proteins
nucleic acids
carbohydrates
lipids

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28
Q

what are inorganic substances

A

water

Ions (sodium, potassium, chloride, calcium, magnesium, bicarbonate, hydrogen phosphate)

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29
Q

what does a lysosome do

A

breakdown of proteins and other molecules

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30
Q

what does the nucleus do

A

contains DNA

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31
Q

what does RNA do

A

transcription & translation of proteins

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32
Q

What do ribosomes do

A

proteins production

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33
Q

what does the endoplasmic reticulum do

A

synthesis and storage

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34
Q

what does Golgi apparatus do

A

secretion of proteins

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35
Q

what does mitochondria do

A

site of metabolic processes

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36
Q

define metabolism

A

the sum of the chemical reactions occurring in a living organism/ part of it

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37
Q

what is the symbol for entropy

A

S

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38
Q

what does an increase in order do to entropy

A

decrease in entropy

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39
Q

what does a decrease in order do to entropy

A

increase in entropy

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40
Q

What is delta G

A

Free energy

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41
Q

What is the free energy equation

A

deltaG = DeltaH - TdeltaS

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42
Q

what is delta H

A

enthalpy (bond energy)

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43
Q

What is T delta S

A

Temp x entropy

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44
Q

what effects deltaG

A

Temperature
Pressure
Conc of reactants & products
pH

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45
Q

What are standard conditions for free energy change reaction

A

25 degrees
1atm pressure
pH 7

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46
Q

what is exergonic

A

free energy of products is lower than the reactants

therefore favoured

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47
Q

what is endergonic

A

free energy of products is higher than reactants

therefore unfavoured

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48
Q

What is equilibrium

A

dynamic state whereby energy of products and reactants is equal

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49
Q

When a compound accepts oxygen what happens

A

it is oxidised

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50
Q

When a compound loses oxygen what happens

A

it is reduced

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51
Q

When a compound loses hydrogen what happens

A

it is oxidised

catabolism

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52
Q

When a compound accepts hydrogen what happens

A

it is reduced

anabolism

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53
Q

how many hydroxyl groups do carbohydrates contain

A

at least 2 hydroxyl groups

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54
Q

what are monosaccharides

A

simplest carbohydrates

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55
Q

Function of carbs??

A

offer cells external protection (cellulose)

assist cells in recognising molecules when attached to proteins and lipids

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56
Q

what are ogliosaccharides

A

when 2-10 monosaccharides link covalently

linkages are glycosidic bonds

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57
Q

what is sucrose made from

A

glucose and fructose

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58
Q

what is lactose made from

A

galactose and glucose

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59
Q

what is maltose made from

A

2x alpha glucose

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60
Q

what are polysaccharides

A

formed from 10+ monosaccharides

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61
Q

give 2 examples of polysaccharides

A

cellulose

starch

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62
Q

what do lipids exist as

A

exist as large tissue (adipose)

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63
Q

what is a common feature of lipids

A

low solubility in water

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64
Q

what is a saturated fat

A

single bonds only (palimate)

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65
Q

what is an unsaturated fat

A

single and double bonds

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66
Q

what are fatty acids linked by

A

ester bonds

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67
Q

role of vitamin B1

A

thiamine

found in active site of pyruvate dehydrogenase

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68
Q

role of vitamin B6

A

coenzymes for aminotransferases and neurotransmitters

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69
Q

role of vitamin B12

A

serves as an enzyme in fatty acid processing

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70
Q

role of vitamin A

A

contained within the retinas of the eye

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71
Q

role of vitamin B2

A

riboflavin

precursor of coenzymes for redox reactions

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72
Q

role of vitamin D

A

involved in calcium absorption - bone health

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73
Q

role of sodium

A

Main cation in extracellular fluids
Essential for electrical transmission in nerves and muscle
Maintains water content in various compartments of the body

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74
Q

role of calcium

A

critical component of bones and blood clotting

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75
Q

role of potassium

A

interacts with Na+ to maintain fluid balance and electrical impulses

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76
Q

role of magnesium

A

cofactor for hundreds of enzymes

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77
Q

role of iron

A

embedded in proteins handling oxygen and the electron transport chain

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78
Q

role of copper

A

is a cofactor for cytochrome, a key component in the electron transport chain

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79
Q

role of zinc

A

sits in the active site of around 200 enzymes, one of which helping get rid of co2

80
Q

role of manganese

A

a cofactor for over 100 enzymes involved in metabolism

81
Q

role of chloride

A

main anion of extracellular fluids. it interacts with Na in maintenance of fluid balance and electrical charges across cell membranes

used in production of HCL

82
Q

role of phosphorus

A

phosphoryl groups covalently attached to vast array of biological compounds (nucleic acids, high energy phosphates)

83
Q

what is transcription

A

DNA becoming mRNA

84
Q

what is translation

A

mRNA becoming a protein

85
Q

how many different types of protein in human body

A

74,000

86
Q

what are the 3 parts to an amino acid

A

amino group
carboxyl group
side chain/ variable group

87
Q

what gives an amino acid its identity

A

the side chain/ variable group

88
Q

how are amino acids joined

A

covalently through peptide bonds

89
Q

what is it called when multiple amino acids are joined together

A

a polypeptide chain

90
Q

what is primary structure of a protein

A

the basic amino acid sequence that determines protein shape and function
The simplest structure

91
Q

what is secondary structure of a protein

A

peptides fold in complex ways due to hydrogen bonds

alpha helix & beta pleated sheet

92
Q

what is tertiary structure of a protein

A

hydrogen bonds
electrostatic bonds
van der Waals interactions
disulphide bonds

93
Q

what are electrostatic bonds between

A

positive and negatively charged groups

94
Q

what are ionic bonds between

A

positive and negatively charged groups

95
Q

what are van der Waals interactions between

A

a non covalent attraction due to movement of ions in atomic or molecular orbitals

96
Q

what is quaternary structure of a protein

A

many proteins contain subunits that link together via the same interactions

97
Q

what causes the denaturation of proteins

A

environmental factors such as heat/ acidity which can alter/ break forces

98
Q

what are enzymes

A

essential catalysts that accelerate metabolic reactions

99
Q

what are the 3 main features of enzymes

A

speed up reactions

display high specificity- each enzyme catalyses one reaction

catalytic power is regulated - speed of reaction is subject to a variety of factors

100
Q

what are the limiting factors affecting rate of enzyme reactions

A

Substrate availability
Enzyme concentration
Temperature
pH

101
Q

What are the purines

A

adenine & guanine

102
Q

What are the pyrimidines

A

thymine (uracil in RNA)

cytosine

103
Q

what are nucleotides joined together by

A

phosphodiester bonds

104
Q

is DNA double or single stranded

A

double helix

105
Q

is RNA double or single stranded

A

single stranded

106
Q

describe DNA replication

A
  1. separate strands
    DNA helices breaks H bonds to unzip molecule
  2. primer binding
    a small strip of RNA primer kickstarts replication
  3. elongation
    DNA polymerase adds complimentary base pairs in the 5- to 3- direction
  4. termination
    exonuclease removes original primers and then bases are re added to complete a new DNA double helix
107
Q

what are the 3 types of RNA

A

mRNA (messenger, which decodes DNA)
rRNA (ribosomal, which decodes mRNA)
tRNA (transfer, which facilitates protein formation)

108
Q

what are promotors

A

DNA region next to transcription site that docks RNA polymerase

109
Q

what are enhancers

A

DNA regions that attract the transcription factor complex proteins

110
Q

what is the trasncription factor complex

A

proteins that regulate the rate of mRNA formation

111
Q

what are introns

A

non coding regions

112
Q

what are exons

A

coding regions

113
Q

describe translation

A

mRNA binds to subunit of rRNA where it is decoded

3 base sequence on mRNA is called a codon

this codon compliments an anticodon on a tRNA molecule

this binds to large subunit of mRNA holding an amino acid

allowing formation of a polypeptide chain via peptide bonds

ribosome moves along mRNA 5- to 3-

peptide bond formed between each amino acid

golgi apparatus modifies proteins & secreted in vesicles

114
Q

describe how to measure total protein abundance via spectrophotometry

A

Bradford essay
protein mixed with blue dye called coomassie blue
in acidic conditions this results in a colour change brown-blue

115
Q

what is the western blot

A

commonly used to detect a specific protein in a tissue homogenate or protein extract

116
Q

what does Eliza testing stand for

A

enzyme linked immunosorbent assay

117
Q

how does Eliza testing work

A

capture antibody and bind to well

add sample

wash microplate

add detection antibody

wash microplate

add substrate

read microplane

calculate results

118
Q

is the myocyte single or multinucleated

A

multi nucleated due to fusion of myoblasts during development

119
Q

can muscle fibres spontaneously contract

A

yes

120
Q

what are the thick filaments called

A

myosin

121
Q

what are thin filaments called

A

actin, tropomyosin, troponin

122
Q

what is the m line made from

A

myosin and M protein

123
Q

what is the Z line made from

A

a-actinin (alpha actinin)

124
Q

what happens to the lengths of the filaments when the sarcomere contracts

A

they DO NOT change length

but the OVERLAP INCREASES

125
Q

How is contraction caused in the muscle

A

by thick myosin and thin actin filaments sliding over each other

126
Q

describe myosin

A

very large & abundant in muscle

consists of 2 large heavy chains & 2 small light chains

127
Q

describe actin

A

main component of thin filaments
exists in 2 forms- G actin (globular) & F actin (fibrous)
tropomyosin and troponin attach to F actin

128
Q

what happens to actin and myosin at rest

A

no binding

129
Q

what part of myosin binds to actin

A

myosin head binds to actin

130
Q

where on the the filament does myosin bind to actin

A

S1
causing a conformational change
creating a lever arm and power stroke happens generating force for contraction

131
Q

what ion controls muscle contraction

A

calcium

132
Q

how does calcium control muscle contraction

A

it permits the binding of myosin to F actin via troponin and tropomyosin

133
Q

what is special about the acetylcholine receptor

A

it is ligand gated

134
Q

what does ligand gated mean

A

it only changes its shape when interacting with its ligand (acetylcholine)

135
Q

anabolic reactions can also be known as

A

endergonic

136
Q

catabolic reactions are also known as

A

exergonic

137
Q

what does myokinase do

A

add phosphate groups

138
Q

is the myokinase reaction aerobic or anaerobic

A

anaerobic

139
Q

what does creatine kinase (CK) do

A

can rapidly reform ATP

140
Q

Are synthesis reactions anabolic or catabolic

A

anabolic eg- condensation

141
Q

are breakdown reactions anabolic or catabolic

A

catabolic eg- hydrolysis

142
Q

is glycolysis aerobic or anaerobic

A

anaerobic

143
Q

what are the reactants of glycolysis

A

glucose

144
Q

what are the products of glycolysis

A

2x pyruvate & NADH

145
Q

how many ATP molecules are generated in glycolysis

A

2 atp molecules

146
Q

what does exercise do to glycolysis and how

A

exercise speeds up glycolysis

  1. substrate availability
  2. physiological factors
  3. cellular factors
  4. molecular factors
147
Q

what are the reactants of the Krebs cycle

A

acetyl coA

148
Q

what are the products if the Krebs cycle

A

2 ATP
6 NADH
2 FADH2
8 H+

149
Q

Is the Krebs cycle aerobic or anaerobic

A

aerobic pathway

150
Q

where does the Krebs cycle take place

A

mitochondrial matrix

151
Q

where does glycolysis take place

A

cytosol

152
Q

What happens to Gibbs free energy when electrons are transferred

A

Gibbs free energy falls as electrons are transferred to FADH and NAD+ during glycolysis and Krebs cycle

153
Q

what are reactants of oxidative phosphorylation

A

8 NADH

4 FADH2

154
Q

what are products of oxidative phosphorylation

A

26 atp
6Co2
6H20

155
Q

is oxidative phosphorylation aerobic or anaerobic

A

aerobic

156
Q

what is gluconeogenesis

A

carbon skeletons from other molecules can be used to synthesise glucose for energy provision in a muscle

157
Q

what helps digest protein in the stomach

A

pepsin enzyme

Hydrochloric acid

158
Q

how much of body % is protein in men

A

16%

159
Q

how much of body % is protein in women

A

14%

160
Q

how many of the 20 amino acids are glucogenic

A

14

161
Q

how many of the 20 amino acids are ketogenic

A

2

162
Q

how many of the 20 amino acids are glutogenic and ketogenic

A

4

163
Q

is transamination reversible

A

yes

164
Q

what is transamination

A

the transfer of one amino group from one molecule to another
catalysed by enzyme aminotransferase

165
Q

what is deamination and what does it form

A

the amino acid removal and loss of its amino group

forms ammonia which is toxic (so gets converted into urea in liver and then excreted)

166
Q

what does FSR stand for

A

fractional synthetic rate

167
Q

what are lipids

A

Diverse biological compounds, characterised by low solubility in water

168
Q

what makes up a phospholipid

A

glycerol & 2 fatty acids

169
Q

what does amphipathic mean in relation to phospholipids

A

one end is hydrophobic

one end is hydrophilic

170
Q

what is a triacylglycerol made of

A

one glycerol unit

3 fatty acids

171
Q

what are chylomicrons

A 
a class of lipoprotein 
transport of insoluble triacylglycerol
172
Q

where does breakdown of triacylglycerol happen

A

in cytosol

173
Q

where does synthesis of triacylglycerol happen

A

in cytosol

174
Q

what is lipolysis affected by

A

epinephrine both increases and decreases lipolysis

insulin reduces lipolysis

175
Q

how are fatty acids degraded

A

through the pathway of beta oxidation in the mitochondria

176
Q

how are lipids transported

A

in lipoproteins

177
Q

what does exercise do to fatty acid oxidation

A

speeds it up

178
Q

what is the energy yield of ATP-PC system

A

low

179
Q

what is the energy yield of anaerobic system

A

medium

180
Q

what is the energy yield of the aerobic system

A

high

181
Q

what is the power of the ATP-PC system

A

High

182
Q

what is the power of the anaerobic system

A

medium

183
Q

what is the power of the aerobic system

A

low

184
Q

how long does the ATP-PC system last

A

7 seconds

185
Q

how long does the anaerobic system last

A

7-60s

186
Q

how long does the aerobic system last

A

above 60s

187
Q

is loosing electrons oxidation or reduction

A

oxidation

OILRIG

188
Q

Is gaining electrons oxidation or reduction

A

redution

OILRIG

189
Q

what Is the non specific part of the immune system called

A

innate immune system

190
Q

what Is the specific part of the immune system called

A

acquired/ adaptive immune system

191
Q

what is one of the main functions of the immune system

A

to be able to recognise self vs non self

192
Q

what responses come under adaptive/ specific Immune system

A 
cell mediated response (T cells)
Humoral response (B cells)
193
Q

what responses come under innate/ non specific Immune system

A 
blood borne (phagocytes)
Physical barriers (skin, saliva, yucas, stomach, tears)
194
Q

what do T cells do

A

T cells release cytokine proteins which assist with killing infected cells

195
Q

what do B cells do

A

can trigger release of antibodies

can differentiate into plasma cells to produce antibodies

SPORT SCIENCE (9 decks)

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