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PA > Module 2: Chemistry And Biochemistry > Flashcards

Module 2: Chemistry And Biochemistry Flashcards

1
Q

3 types of mixtures

A

Solutions, colloid, suspensions

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2
Q

Solutions

A

Solute particles are very tiny, do not settle out or scatter light. Tends to not have any color to it.

e.g., mineral water

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3
Q

Colloid

A

Solute particles are larger than in a solution and scatter light; do not settle out (proteins). Do have color to it.

e.g., jello-o

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4
Q

Suspension

A

Solute particles are very large, settle out, and may scatter light e.g. Blood

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5
Q

What are the ways we can note the concentrations of a solution?

A

% (D5 = 5% dextrose solution) *IV fluid

mg/dL or mg/L

molarity (mmol/L)

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6
Q

1 mol =

A

of grams of an element/compound equal to atomic weight of that substance

– this gives equal number of particles in the solution

avogadro’s number

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7
Q

Molarity

A

1 mole dissolved in enough solvent to give IL volume

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8
Q

Molarity (M) of a solution is expressed in

A

Moles of solute/liters of solution

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9
Q

Molality (m) is expressed in

A

Moles of solute I mass of solvent (kg)

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10
Q

Molality

A

I mole dissolved in IL of solvent

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11
Q

Biological solutions are - solutions

A

Molal

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12
Q

Bonding occurs between

A

Electrons in the valence shell

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13
Q

How many electrons do most elements want

A

8

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14
Q

How many elections does hydrogen want

A

2

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15
Q

How can we make a complete shell

A

In order to make a complete shell, we can either lose extra electrons to go down to the next shell, or we can add electrons to the outer shell to make it complete

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16
Q

Types of chemical bonds

A

Ionic
–Anion vs cation
–Salts

Covalent
–Nonpolar
–Polar
–Hydrogen bonds

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17
Q

What happens in ionic bonding

A

Electrons are transferred from one element to another

Causes them to have a charge (either +/-) depending if they lost or gained an electron

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18
Q

What happens in covalent bonding

A

Electrons are shared

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19
Q

What happens in covalent bonding

A

Electrons are shared

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20
Q

Example of ionic bond

A

Sodium Chloride (NaCl)

Sodium has 1 extra electron in its outer shell, so it loses it and drops it down to a full outer shell at the next level

Chlorine has 7 shell electrons in its outer shell, it wants to gain another electron to make its outer shell 8 and complete

Sodium becomes + chlorine -

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21
Q

Example of ionic bond

A

Sodium Chloride (NaCl)

Sodium has 1 extra electron in its outer shell, so it loses it and drops it down to a full outer shell at the next level

Chlorine has 7 shell electrons in its outer shell, it wants to gain another electron to make its outer shell 8 and complete

Sodium becomes + chlorine -

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22
Q

Example of a covalent bond

A

Methane CH4

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23
Q

Nonpolar covalent bonds have_______sharing

A

Equal e.g. Co2

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24
Q

Polar covalent bonds have______ sharing

A

Unequal

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25
Q

Nonpolar vs. Polar examples

A

Nonpolar: CO2, methane

Polar: water, ammonia

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26
Q

Polar things like to group together, non polar things like to group together… Why does this cause issues?

A

Causes issues when it comes to things in the bloodstream

This is because polar molecules tend to form slight bonds between each other

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27
Q

What does hydrogen bonding do in H20?

A

It helps give water its surface tension, it also helps form grouping.

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28
Q

Polar vs nonpolar molecules in blood

A

Nonpolar molecules e.g., fats have to find themselves in a polar environment with water.

***hydrophobic

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29
Q

How to more non polar molecules inthe bloodstream

A

Carrier proteins

or

Fat soluble (sequester the non polar things away from the water)

Think of oil and vinegar salad dressing

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30
Q

Types of chemical reactions

A

Synthesis/combination
(anabolic)
endergonic (uses energy)

Decomposition (catabolic)
Exergonic (releases energy)

Exchange/displacement
(combined)

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31
Q

Example of synthesis (anabolic) reaction

A

Dehydration synthesis

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32
Q

Ex ample of decomposition (catabolic) reaction

A

Hydrolysis

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33
Q

Example of exchange/displacement reaction

A

Oxidation-reduction (electron-donor acceptor)

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34
Q

Synthesis (combination) reaction

A

A reaction in which two or more substances combine to form a new compound

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35
Q

Decomposition reaction

A

A reaction in which a single compound breaks down to form two or more simpler substances

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36
Q

Exchange (displacement) reaction

A

Bonds are both made and broken

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37
Q

Rate of reactions is affected by

A

Body temperature
Concentration
Reactant size
Catalysts (ex: enzymes)

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38
Q

Acids

A

Acids release H+

e.g., HCl (stomach acid), H2CO3 (found in bloodstream)

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39
Q

Bases

A

Bases absorb H+

e.g.,HCO3 , NH3 (ammonia)

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40
Q

pH scale

A

Measurement of H+
concentration in a solution (how acidic or basic a solution is)

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41
Q

Solutions with lower concentrations of hydrogen ions have ______ pHs and are considered _______

A

Higher, basic

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42
Q

Solutions with higher concentrations of hydrogen ions have ______ pHs and are considered _______

A

Lower, acidic

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43
Q

Solutions with higher concentrations of hydrogen ions have ______ pHs and are considered _______

A

Lower, acidic

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44
Q

Negative logarithmic scale

A

Negative = lower numbers = higher
concentration

Logarithmic = each unit =10-fold change
(pH 6 is 10X higher concentration than pH
7)

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45
Q

Arterial pH

A

7.35- 7.45

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46
Q

Denaturation

A

Changes in pH can cause
disruption in protein
structure by disrupting
hydrogen bonding

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47
Q

What happens W denaturation

A

Denature hydrogen bonding, so it can denature our proteins and render them nonfunctional. Causing our enzymes, hormones, etc to stop working.

Eventually will die if too basic or too acidic.

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48
Q

Buffers

A

prevent significant/rapid pH changes

a buffer will absorb the extra acid and neutralize it. if you do not have enough acid, that same compound can dissociate and form acid.

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49
Q

What serves as buffers intracellularly?

A

phosphates, hemoglobins, other proteins. resist pH changes inside the cells.

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50
Q

What serves as buffers extracellularly

A

HCO3, plasma

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51
Q

What server as a buffer for both Intra/extracellular

A

Amino acids

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52
Q

What server as a buffer for both Intra/extracellular

A

Amino acids

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53
Q

Carbohydrates function

A

Energy source (it’s all about those hydrogens) ***the hydrogen are used by the mitochondria to flow through ATP synthase enzyme and form ATP. All about getting the hydrogens off of the carbohydrates and moving them over to the mitochondria.

Cell-cell interactions, on surface of cell membrane
-Glycosylated (proteins with sugars attached) molecules on cell surfaces
-form signaling molecules that help signal to other cells

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54
Q

Structure of carbohydrates

A

C,H,O in a 1:2:1 ratio

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55
Q

(CH20)n

A

“Hydrated carbon” (water +carbon)

56
Q

monosaccharides

A

Monomers of carbohydrates (5 or 6 sided ring of carbon with an oxygen in the last position)

hexose or pentose sugars

simple sugars (glucose, fructose, galactose, deoxyribose, ribose)

57
Q

Disaccharides

A

Consist of two linked monosaccharides

Sucrose, maltose, lactose

58
Q

Polysaccharides

A

Long chains (polymers) of linked monosaccharides

Glycogen

59
Q

Carbohydrates are added to many molecules for ____

A

Cell communication

60
Q

Carbohydrates are added to the surface of cells for recognition of ___

A

Self

61
Q

Outer cell membrane ofcarbohydrates

A

Glycocalyx

Glycoplipids, glycophingolipids, glycoproteins

62
Q

Glycocalyx

A

sticky/sugary coating surrounding the cell made up of carbohydrate proteins and sugars

63
Q

Glyco means

A

Sugar

64
Q

How is it indicated that disruption of the glycocalyx is involved in disease processes?

A

The disruption of this in chronic inflammation can make it easier for viruses to invade cells, due to the glycocalyx being disrupted.

65
Q

How is it indicated that disruption of the glycocalyx is involved in disease processes?

A

The disruption of this in chronic inflammation can make it easier for viruses to invade cells, due to the glycocalyx being disrupted.

66
Q

What are lipids

A

Lipids are macromolecules made of fatty acid monomers

67
Q

Lipids

A

Longer chains/rings of hydrocarbons (ch)
nonpolar

68
Q

Main types of lipids

A

Triglycerides

Phospholipids

Steroids and waxes

69
Q

Lipids are

A

Hydrophobic, non-polar

70
Q

Functions of lipids (triglycerides)

A

Long term energy storage

Protection of organs

Insulation

71
Q

Functions of lipids (phospholipids, steroids)

A

Cell membrane

72
Q

Functions of lipids (steroids)

A

Nonpolar hormones

73
Q

Functions of lipids (glycolipids, eicosanoids)

A

Cell-cell interactions

74
Q

Functions of lipids (lipoproteins)

A

Transport of nonpolar substances

75
Q

Triglycerides

A

1 glycerol + 3 fatty acids

76
Q

Types of triglycerides

A

Saturated and unsaturated

77
Q

Saturated triglycerides

A

All singe bonds
solid (i.e. butter)

Very straight chain, easier to pack molecules close together.

78
Q

Unsaturated triglyceride

A

One or more double bonds
liquid (i.e. oil)

Puts a kink in the chains, harder to pack molecules together

79
Q

What are omega-3 and omega-6 fats?

A

Omega-n refers to the number (n) of the carbon atom with the first double bond from the methyl end

80
Q

What are omega-3 and omega-6 fatty important with?

A

Cardiovascular health

Can help prevent acrosclerosis, help regulate level of triglycerides in bloodstream

e.g., prescriptions

81
Q

Phospholipids

A

1 glycerol + 2 fatty acids + 1 phosphate

One polar portion and one non polar portion

82
Q

What happens to phospholipids in a polar environment?

A

In a polar environment, phospholipids line up and form a semi-permeable membrane. This is how we form the cell membranes.

83
Q

Membranes (phospholipids)

A

Outer cell membrane
Inner organelle membranes

84
Q

Phospholipid structure

A

Hydrophilic head and hydrophobic tail (helps form a non polar membrane)

85
Q

What happens to phospholipids in a watery environment?

A

In a watery environment, phospholipids automatically line up with their heads facing the water on either side, and their hydrophobic tails “hiding” away from the water

86
Q

Steroids

A

Derived from cholesterol (4 rings)

Non polar

Need transport in bloodstream (hormones)

87
Q

How are steroid hormones formed

A

Different steroids have different groups attached to the 4-ring backbone.

***cholesterol is the basis for all steroids formed in the body

88
Q

Ex of steroid hormones

A

Testosterone, estrogen, progesterone, cortisol, aldosterone, vitamin D

89
Q

Steroid uses

A

Hormones

Membrane structure (esp cholesterol. embedded in bipolar layer to give fluidity to cell membrane)

Bile salts (made by liver, stored in gallbladder, released into small intestine. takes fats and foods we eat and sequester it into lipid droplets. makes it easier to digest and transport in the body)

Vitamins

Eicosanoids
==Derived from arachidonic acid
e.g., prostaglandins
==Involved in inflammation, tissue damage response

90
Q

What do prostaglandin do

A

Mediates inflammation

91
Q

A lot of the hormones we find in the body are:

A

Non polar steroid hormones

So they require some sort of transport in the blood, but then move very easily through the membrane into the cells. Therefore can affect all cells in the body.

92
Q

Proteins are

A

Chains of AA

93
Q

Proteins are

A

Chains of AA

94
Q

Basic AA #?

A

20

95
Q

AA structure

A

A central carbon, a hydrogen, carboxyl group, amino group, and r group

96
Q

What causes amino acids to be different?

A

R group

97
Q

What are post - translational changes

A

Addition of chemical groups
Addition of larger molecules
Changes of amino acid structure

98
Q

Post translational changes info

A

Amino acids can undergo post-translational changes. These changes occur on the R-group and form a completely new amino acid.
***

Arginine is an example, sometimes changes into citrulline

99
Q

Primary structure

A

The sequence of amino acids forms the polypeptide chain. R groups are on opposite sides of each other.

100
Q

Secondary structure

A

The primary chain forms spirals (alpha-helices) and sheets (beta-sheets).

101
Q

Secondary structure

A

The primary chain forms spirals (alpha-helices) and sheets (beta-sheets).

102
Q

Tertiary structure

A

Superimposed on secondary structure, alpha helices and/or beta sheets are folded up to form a compact globular molecule held together by intermolecular bonds.

a three-dimensional combination of α-helices and β-sheets

103
Q

Tertiary structure

A

Superimposed on secondary structure, alpha helices and/or beta sheets are folded up to form a compact globular molecule held together by intermolecular bonds.

a three-dimensional combination of α-helices and β-sheets

104
Q

Quaternary structure

A

Two or more polypeptide chains, each with its own tertiary structure, combine to form a functional protein.

e.g., hemoglobin

105
Q

Function of structural proteins

A

Mechanical support

example: collagen, found in all connective tissue, is the single most abundant protein in the body. It is responsible for the tensile strength of bones, tendons, and ligaments. Collagen basically helps form shape.

106
Q

Function of enzyme proteins

A

Catalysts. Protein enzymes are essential for virtually every biochemical reaction in the body.

example: disaccharidases hydrolyze disaccharides, proteases hydrolyze proteins, and oxidases oxide food fuels.

107
Q

What did older enzymes end in?

A
  • in
108
Q

What do newer enzymes end in

A

-ase

109
Q

What does the naming of enzymes do?

A

The newer names tell what they do. Older names do not necessarily tell you (renin for example).

e.g., alcohol dehydrogenase. It takes away an hydrogen from alcohol.

110
Q

What are proenzymes

A

Inactive enzymes

The enzyme is premade and has a “inactive cap” on its active cite. When the enzyme is needed another enzyme cleaves off the cap and the enzyme is not inactive and can be used.

111
Q

Competitive inhibition

A

Substance that resembles the normal substrate competes with the substrate for the active site. Blocking the substrate from binding. Reversible.

112
Q

Noncompetitive inhibition

A

Inhibitor binds elsewhere on the enzyme; alters active site so that the substrate cannot bind.

Induces an irreversible shape change to the active site. Becomes completely nonfunctional.

113
Q

Transport proteins

A

Moving substances

membrane transporters or sebum transports across the plasma membrane

example: hemoglobin transports oxygen in blood. Some plasma membrane proteins transport substance (such as ions) across the plasma membrane

114
Q

Contraction/movement proteins

A

Movement

example: actin and myosin cause muscles cell contraction and function in cell division in all cell types.

115
Q

Communication proteins

A

Transmitting signals between cells. Can act as chemical messengers or as receptors in the plasma membrane

example: insulin (a protein) acts as its receptor to regulate blood sugar levels.

116
Q

Communication proteins

A

Transmitting signals between cells. Can act as chemical messengers or as receptors in the plasma membrane

example: insulin (a protein) acts as its receptor to regulate blood sugar levels.

117
Q

Types of communication proteins

A

Peptide hormones

Membrane receptors

Neurotransmitters

118
Q

Energy of activation (EA)

A

The amount of energy that reactants must absorb before a chemical reaction will start

119
Q

Immune/defense proteins

A

Prevent and protect against pathogen attack/disease

example: antibodies released by certain immune cells are specialized proteins that bind and inactive foreign substances (e.g., bacteria, toxins, viruses).

120
Q

What are immune proteins

A

Antibodies - made against a specific virus/bacteria.

Complement - nonspecific, does not matter what invader is in.

121
Q

Nucleic acids are

A

Largest molecules in the body

122
Q

What are nucleic acids made of

A

Nucleotides

123
Q

What are nucleic acids involved in

A

Protein synthesis

124
Q

Names of nucleotides

A

Adenine
Thymine
Cytosine
Guanine
Uracil

125
Q

What is DNA

A

Deoxyribonucleic Acid

Genetic code that gives the sequence of information on how to make the proteins.

Replicates and stores genetic information

126
Q

RNA

A

Ribonucleic acid. Translates the code from DNA into the protein. Carry out instructions encoded in DNA.

Encodes amino acid sequence of all proteins

Strands held together by hydrogen bonds

127
Q

RNA

A

Ribonucleic acid. Translates the code from DNA into the protein. Carry out instructions encoded in DNA.

Encodes amino acid sequence of all proteins

Strands held together by hydrogen bonds

128
Q

What is RNA

A

Copy of a gene used to make protein

1 Strand

129
Q

What is RNA

A

Copy of a gene used to make protein

1 Strand

130
Q

Parts of a nucleotide

A

Sugar, phosphate, nitrogen base

131
Q

ATP

A

adenosine + phosphate

adenosine triphosphate

what we use to speed up reactions

132
Q

ATP → ADP + Pi

A

Releases energy
==”spring”

Energy transfer to enzyme-substrate complex to help complete the reaction

133
Q

Describe the fundamental composition of matter.

A

The atom
Solids, liquids, gases

134
Q

4 most abundant elements in the body

A

Oxygen, carbon, hydrogen, nitrogen

135
Q

Distinguish between ionic bonds, covalent bonds, and hydrogen bonds.

A

ionic bond attraction between an anion and a cation

covalent bond chemical bond in which two atoms share electrons, thereby completing their valence shells

hydrogen bond dipole-dipole bond in which a hydrogen atom covalently bonded to an electronegative atom is weakly
attracted to a second electronegative atom

136
Q

Explain how energy is invested, stored, and released via chemical reactions, particularly those reactions that are critical to life.

A

In the human body, potential energy is stored in the bonds between atoms and molecules. Chemical energy is the form of potential energy in which energy is stored in chemical bonds. When those bonds are formed, chemical energy is invested, and when they break, chemical energy is released. Notice that chemical energy, like all energy, is neither created nor destroyed; rather, it is converted from one form to another.

Chemical reactions that release more energy than they absorb are characterized as exergonic. The catabolism of the foods in your energy bar is an example. Some of the chemical energy stored in the bar is absorbed into molecules your body uses for fuel, but some of it is released-for example, as heat. In contrast, chemical reactions that absorb more energy than they release are endergonic.

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