Module 2: Chemistry And Biochemistry Flashcards
(136 cards)
1
Q
3 types of mixtures
A
Solutions, colloid, suspensions
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
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
4
Q
Suspension
A
Solute particles are very large, settle out, and may scatter light e.g. Blood
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)
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
7
Q
Molarity
A
1 mole dissolved in enough solvent to give IL volume
8
Q
Molarity (M) of a solution is expressed in
A
Moles of solute/liters of solution
9
Q
Molality (m) is expressed in
A
Moles of solute I mass of solvent (kg)
10
Q
Molality
A
I mole dissolved in IL of solvent
11
Q
Biological solutions are - solutions
A
Molal
12
Q
Bonding occurs between
A
Electrons in the valence shell
13
Q
How many electrons do most elements want
A
8
14
Q
How many elections does hydrogen want
A
2
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
16
Q
Types of chemical bonds
A
Ionic
–Anion vs cation
–Salts
Covalent
–Nonpolar
–Polar
–Hydrogen bonds
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
18
Q
What happens in covalent bonding
A
Electrons are shared
19
Q
What happens in covalent bonding
A
Electrons are shared
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 -
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 -
22
Q
Example of a covalent bond
A
Methane CH4
23
Q
Nonpolar covalent bonds have_______sharing
A
Equal e.g. Co2
24
Q
Polar covalent bonds have______ sharing
A
Unequal
25
Nonpolar vs. Polar examples
Nonpolar: CO2, methane
Polar: water, ammonia
26
Polar things like to group together, non polar things like to group together... Why does this cause issues?
Causes issues when it comes to things in the bloodstream
This is because polar molecules tend to form slight bonds between each other
27
What does hydrogen bonding do in H20?
It helps give water its surface tension, it also helps form grouping.
28
Polar vs nonpolar molecules in blood
Nonpolar molecules e.g., fats have to find themselves in a polar environment with water.
***hydrophobic
29
How to more non polar molecules inthe bloodstream
Carrier proteins
or
Fat soluble (sequester the non polar things away from the water)
Think of oil and vinegar salad dressing
30
Types of chemical reactions
Synthesis/combination
(anabolic)
endergonic (uses energy)
Decomposition (catabolic)
Exergonic (releases energy)
Exchange/displacement
(combined)
31
Example of synthesis (anabolic) reaction
Dehydration synthesis
32
Ex ample of decomposition (catabolic) reaction
Hydrolysis
33
Example of exchange/displacement reaction
Oxidation-reduction (electron-donor acceptor)
34
Synthesis (combination) reaction
A reaction in which two or more substances combine to form a new compound
35
Decomposition reaction
A reaction in which a single compound breaks down to form two or more simpler substances
36
Exchange (displacement) reaction
Bonds are both made and broken
37
Rate of reactions is affected by
Body temperature
Concentration
Reactant size
Catalysts (ex: enzymes)
38
Acids
Acids release H+
e.g., HCl (stomach acid), H2CO3 (found in bloodstream)
39
Bases
Bases absorb H+
e.g.,HCO3 , NH3 (ammonia)
40
pH scale
Measurement of H+
concentration in a solution (how acidic or basic a solution is)
41
Solutions with lower concentrations of hydrogen ions have ______ pHs and are considered _______
Higher, basic
42
Solutions with higher concentrations of hydrogen ions have ______ pHs and are considered _______
Lower, acidic
43
Solutions with higher concentrations of hydrogen ions have ______ pHs and are considered _______
Lower, acidic
44
Negative logarithmic scale
Negative = lower numbers = higher
concentration
Logarithmic = each unit =10-fold change
(pH 6 is 10X higher concentration than pH
7)
45
Arterial pH
7.35- 7.45
46
Denaturation
Changes in pH can cause
disruption in protein
structure by disrupting
hydrogen bonding
47
What happens W denaturation
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.
48
Buffers
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.
49
What serves as buffers intracellularly?
phosphates, hemoglobins, other proteins. resist pH changes inside the cells.
50
What serves as buffers extracellularly
HCO3, plasma
51
What server as a buffer for both Intra/extracellular
Amino acids
52
What server as a buffer for both Intra/extracellular
Amino acids
53
Carbohydrates function
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
54
Structure of carbohydrates
C,H,O in a 1:2:1 ratio
55
(CH20)n
"Hydrated carbon" (water +carbon)
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monosaccharides
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
Disaccharides
Consist of two linked monosaccharides
Sucrose, maltose, lactose
58
Polysaccharides
Long chains (polymers) of linked monosaccharides
Glycogen
59
Carbohydrates are added to many molecules for ____
Cell communication
60
Carbohydrates are added to the surface of cells for recognition of ___
Self
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Outer cell membrane ofcarbohydrates
Glycocalyx
Glycoplipids, glycophingolipids, glycoproteins
62
Glycocalyx
sticky/sugary coating surrounding the cell made up of carbohydrate proteins and sugars
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Glyco means
Sugar
64
How is it indicated that disruption of the glycocalyx is involved in disease processes?
The disruption of this in chronic inflammation can make it easier for viruses to invade cells, due to the glycocalyx being disrupted.
65
How is it indicated that disruption of the glycocalyx is involved in disease processes?
The disruption of this in chronic inflammation can make it easier for viruses to invade cells, due to the glycocalyx being disrupted.
66
What are lipids
Lipids are macromolecules made of fatty acid monomers
67
Lipids
Longer chains/rings of hydrocarbons (ch)
nonpolar
68
Main types of lipids
Triglycerides
Phospholipids
Steroids and waxes
69
Lipids are
Hydrophobic, non-polar
70
Functions of lipids (triglycerides)
Long term energy storage
Protection of organs
Insulation
71
Functions of lipids (phospholipids, steroids)
Cell membrane
72
Functions of lipids (steroids)
Nonpolar hormones
73
Functions of lipids (glycolipids, eicosanoids)
Cell-cell interactions
74
Functions of lipids (lipoproteins)
Transport of nonpolar substances
75
Triglycerides
1 glycerol + 3 fatty acids
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Types of triglycerides
Saturated and unsaturated
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Saturated triglycerides
All singe bonds
solid (i.e. butter)
Very straight chain, easier to pack molecules close together.
78
Unsaturated triglyceride
One or more double bonds
liquid (i.e. oil)
Puts a kink in the chains, harder to pack molecules together
79
What are omega-3 and omega-6 fats?
Omega-n refers to the number (n) of the carbon atom with the first double bond from the methyl end
80
What are omega-3 and omega-6 fatty important with?
Cardiovascular health
Can help prevent acrosclerosis, help regulate level of triglycerides in bloodstream
e.g., prescriptions
81
Phospholipids
1 glycerol + 2 fatty acids + 1 phosphate
One polar portion and one non polar portion
82
What happens to phospholipids in a polar environment?
In a polar environment, phospholipids line up and form a semi-permeable membrane. This is how we form the cell membranes.
83
Membranes (phospholipids)
Outer cell membrane
Inner organelle membranes
84
Phospholipid structure
Hydrophilic head and hydrophobic tail (helps form a non polar membrane)
85
What happens to phospholipids in a watery environment?
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
Steroids
Derived from cholesterol (4 rings)
Non polar
Need transport in bloodstream (hormones)
87
How are steroid hormones formed
Different steroids have different groups attached to the 4-ring backbone.
***cholesterol is the basis for all steroids formed in the body
88
Ex of steroid hormones
Testosterone, estrogen, progesterone, cortisol, aldosterone, vitamin D
89
Steroid uses
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
What do prostaglandin do
Mediates inflammation
91
A lot of the hormones we find in the body are:
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
Proteins are
Chains of AA
93
Proteins are
Chains of AA
94
Basic AA #?
20
95
AA structure
A central carbon, a hydrogen, carboxyl group, amino group, and r group
96
What causes amino acids to be different?
R group
97
What are post - translational changes
Addition of chemical groups
Addition of larger molecules
Changes of amino acid structure
98
Post translational changes info
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
Primary structure
The sequence of amino acids forms the polypeptide chain. R groups are on opposite sides of each other.
100
Secondary structure
The primary chain forms spirals (alpha-helices) and sheets (beta-sheets).
101
Secondary structure
The primary chain forms spirals (alpha-helices) and sheets (beta-sheets).
102
Tertiary structure
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
Tertiary structure
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
Quaternary structure
Two or more polypeptide chains, each with its own tertiary structure, combine to form a functional protein.
e.g., hemoglobin
105
Function of structural proteins
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
Function of enzyme proteins
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
What did older enzymes end in?
- in
108
What do newer enzymes end in
-ase
109
What does the naming of enzymes do?
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
What are proenzymes
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
Competitive inhibition
Substance that resembles the normal substrate competes with the substrate for the active site. Blocking the substrate from binding. Reversible.
112
Noncompetitive inhibition
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
Transport proteins
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
Contraction/movement proteins
Movement
example: actin and myosin cause muscles cell contraction and function in cell division in all cell types.
115
Communication proteins
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
Communication proteins
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
Types of communication proteins
Peptide hormones
Membrane receptors
Neurotransmitters
118
Energy of activation (EA)
The amount of energy that reactants must absorb before a chemical reaction will start
119
Immune/defense proteins
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
What are immune proteins
Antibodies - made against a specific virus/bacteria.
Complement - nonspecific, does not matter what invader is in.
121
Nucleic acids are
Largest molecules in the body
122
What are nucleic acids made of
Nucleotides
123
What are nucleic acids involved in
Protein synthesis
124
Names of nucleotides
Adenine
Thymine
Cytosine
Guanine
Uracil
125
What is DNA
Deoxyribonucleic Acid
Genetic code that gives the sequence of information on how to make the proteins.
Replicates and stores genetic information
126
RNA
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
RNA
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
What is RNA
Copy of a gene used to make protein
1 Strand
129
What is RNA
Copy of a gene used to make protein
1 Strand
130
Parts of a nucleotide
Sugar, phosphate, nitrogen base
131
ATP
adenosine + phosphate
adenosine triphosphate
what we use to speed up reactions
132
ATP → ADP + Pi
Releases energy
=="spring"
Energy transfer to enzyme-substrate complex to help complete the reaction
133
Describe the fundamental composition of matter.
The atom
Solids, liquids, gases
134
4 most abundant elements in the body
Oxygen, carbon, hydrogen, nitrogen
135
Distinguish between ionic bonds, covalent bonds, and hydrogen bonds.
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
Explain how energy is invested, stored, and released via chemical reactions, particularly those reactions that are critical to life.
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.
