Chapters 1, 2, 3, & 6 Flashcards
1
Q
Sequence of chemical reactions in which each reaction is dependent upon the one before
A
Metabolic pathway
2
Q
Energy released by breaking down complex molecules
Ex: digestion, cellular respiration
A
Catabolic
3
Q
Energy used to build more complex molecules
Ex: photosynthesis
A
Anabolic
4
Q
Form of energy cells used to do work and donates 3rd phosphate groups
Hydrolysis Reaction: ATP+H20>ADP+Pi
A
ATP (adenosine triphosphate)
5
Q
When one phosphate group is transferred to another molecule
A
Phosphorylation
6
Q
Using an exergonic reaction to drive an endergonic reaction
A
energy coupling
7
Q
Regulate metabolism; speeds up chemical reactions; AKA catalysts;
A
Enzymes
8
Q
Energy required to start a chemical reaction
A
Activation energy
9
Q
Bonding rules:
A
1-3 e: tends to donate e; becomes positive ion
6-7 e: tends to gain e; becomes negative ion
4-5 e: (sometimes 6) tends to share e; from covalent bonds
10
Q
Outermost electron shell of an atom
A
valence shell
11
Q
When number of protons and electrons aren’t equal
A
Ion
12
Q
Atoms of an element with the same number of protons, but different number of neutrons
A
Isotopes
13
Q
Donating, taking, or sharing electrons
A
Chemical bond
K - 1st level; up to 2 electrons
L - 2nd level; up to 8 electrons
M - 3rd level; up to 8 electrons
14
Q
Number of protons in atom’s nucleus
A
Atomic number
15
Q
Number of protons and neutrons in nucleus
A
Atomic mass
16
Q
Atoms are made up of 3 subatomic particles:
A
Protons (live in nucleus)
Neutrons (live in nucleus)
Electrons (revolve around nucleus)
17
Q
When you have 2+ atoms joined by a chemical bond in fixed ratios
A
Molecules
18
Q
Specific type of molecule whose atoms are different
A
Compound
19
Q
Living organisms are mainly made up of:
A
Carbon
Nitrogen
Oxygen
Hydrogen
20
Q
Elements necessary for life, but aren’t needed in large amounts
Ex: Iodine
A
Trace Elements
21
Q
Smallest units that retain the properties of an element
A
Atom
22
Q
Pure substance that can’t be broken down into simpler substances by ordinary chemical or physical techniques
A
Element
23
Q
Anything that occupies space; made of elements
A
Matter
24
Q
Broadly applicable ideal or hypothesis that has been supported/confirmed by every conceivable test; tested many times by different people but hasn’t been disproven
A
Scientific theory
25
Examples of scientific theories:
Theory of evolution
| Germ theory
26
Make observations to form a general statement
Inductive reasoning
27
Scientific method steps
Observation
Hypothesis
Experiment/ make prediction
Share
28
acquiring knowledge through observations or working out an explanation and testing the explanation through carefully designed experiment
Scientific method
29
Ability to maintain a relatively constant internal environment
Homeostasis
30
2 main types of biological research:
1 - basic research
| 2 - applied research
31
explains natural phenomena or advance collective knowledge; scientist doesn't change anything, only observes
Basic research; observational data
32
usually tries to solve a specific problem; scientists usually change something
Applied research; experimental data
33
Hierarchy of classification
```
Domain
Kingdom
Phylum
Class
Order
Family
Genus
Species
```
34
Organization of life:
Biosphere - Earth
Ecosystems - Community + nonliving things
Community - population of org. living in same place
Population - group living in same place
Multicellular organism - can't survive on own
Cells - building block of life
35
Sequential stages of reproduction & development
life cycle
36
Changes in a population over time
evolution
37
Other organization of life:
Organ system
organ
tissue
cell
38
Different genes in a population are valued differently for survival and reproduction
natural selection
39
species that make good test subjects
mice - medicine
fruit flies - genetics
model organisms
40
Partially hydrophobic; make up cell membranes; keep them flexible without being leaky
phospholipids
41
Natural/non polar/hydrophobic
| Sterol; phytosterol; hormones
Steroids
42
Cholesterol; found in cell membrane
Sterol
43
Plants version of cholesterol
Phytosterol
44
20 different types of amino acids
Regulates metabolism
Helps move things across cell membrane
Used for communication
Protein
45
Every protein has:
N-Terminal End: NH3
| C-Terminal End: COO
46
4 possible levels of protein structure:
Primary
Secondary
Tertiary
Quaternary
47
Sequence of amino acids
Primary structure
48
Twists and turns of amino acid chain
alpha helix - winds in right hand helix
beta strand - folds into zig zag; forms beta sheets
Secondary structure
49
3D folding of protein
| Conformation - most important for function
Tertiary structure
50
Structure for more complex proteins
Quaternary structure
51
Unfolded; its conformation has changed; no longer works
Denaturation
52
If a denatured protein can be returned to its original structure
Renaturation
53
Specialized proteins that fold proteins into their tertiary structure; dictates its function and solubility
Chaperone proteins/chaperonins
54
Long chains of polymers of nucleotides
Nucleic acids
55
1 nucleotide =
1 sugar, 1 phosphate, 1 nitrogenous base
56
Characteristics of life:
```
growth
reproduction
respiration
metabolism
ability to maintain its life
```
57
everything you start with in a chemical equation
Reactant
58
everything you end up with in a chemical equation
Product
59
- Weakest of chemical bonds
- Temporary bond
- Develop over short distances between non polar molecules when electrons accumulate by chance
Van der Waals forces
60
Bonds between atoms of the same molecule
Intramolecular forces
61
bonds between atoms in different molecules
Intermolecular forces
62
- Not strong
- "Easy to break, easy to make"
- usually polar
hydrogen bonds
63
Have as many hydrogens as possible; non polar bc the way they arrange their bonds
Hydrocarbons
64
Love water; polar
hydrophilic
65
hate water; nonpolar
hydrophobic
66
Form when you try to mix polar and non polar substances; excludes nonpolar
Polar associations
67
Form when you try to mix polar and non polar substances; exclude polar
Non polar associations
68
Different changes associated with different regions of the molecule; atom with higher atomic number is stronger
Polar covalent bond
69
Electrons are shared equally; neutral
Non polar covalent bond
70
- When 2 atoms share electrons
- written with dash or colon
- must be bonded @specific angles or locations
- size and shape of molecule dictates its function
Covalent Bond
71
- Opposites attract
- can bond in amy direction
- occur over long distances (longest bond)
- can be different degrees of strength
Ionic bond
72
Releases free energy; anytime chemical bond is broken
Exergonic reaction
73
Gains energy from broken chemical bond
Endergonic reaction
74
Releases energy outside; products have less potential energy bc some energy was lost in reaction
Exothermic reaction
75
Absorbs energy; products have more potential energy bc energy was absorbed
Endothermic reaction
76
Types of Bonds:
Ionic bond
Covalent bond
Hydrogen bond
Van der Waals forces
77
study of energy
thermodynamics
78
Law of thermodynamics
energy can't be created nor destroyed
| entropy is always increasing (chaos)
79
Positively charged ion
Cation
80
Negatively charged ion
Anion
81
Energy in motion
Kinetic energy
82
stored energy
Potential energy
83
Who discovered the structure of DNA?
Watson & Crick
84
What makes us different in a species?
Amount of DNA & sequence of nitrogenous bases
85
Nitrogenous bases:
Pyrimidines & Purines
86
Types of pyrimidines:
Singles ringed: Uracil (U); Thymine (T); Cytosine (C)
87
Types of purines:
Double ringed: Adenine (A); Guanine (G)
88
Chargoff's Rules:
Every nitrogenous base is paired with opposite one.
Adenine paired w/ Thymine
Cytosine paired w/ Guanine
89
Properties of H20
Hydrogen bonding; polarity; good facilitator of chemical reactions
90
Substance that dissolves something else
Solvent
91
Substance being dissolved
Solute
92
Heat energy is absorbed as something is being cooled
Heat evaporation
93
Resistance to rupturing
Surface tension
94
pH scale
0-6: acidic/ has more H+
8-14: basic/ has more OH-
acids are H+ donors & bases are H+ acceptors
95
What is our internal pH?
7.3-7.5
96
Compensate for pH changes by absorbing or releasing H; often weak acids or bases
Buffers
97
If your body is very acidic, use bicarbonate
| If your body is very basic, use carbonic acid
Carbonic Acid- bicarbonate buffer system
98
Things made of Carbon (other than CO2)
Organic
99
Can form up to 4 covalent bonds at once
Tetravalent
100
Includes OH
| is found in alcohol
hydroxyl
101
Includes C=O
If C=O is on end, its aldehyde
If C=O is in middle, its ketone
Carbonyl
102
Include COOH
| Found in vinegar
Carboxyl
103
Includes NH2
Only functional group with nitrogen
Amino acids in protein have amino grouos
Amino
104
Blueprints
Sugar phosphate backbone; sugars bridged with phosphate group through phosphodiester bond
Double helix
DNA (deoxyribose nucleic acid)
105
Single stranded
Uses uracil instead of thymine
Sugar is ribose
RNA (ribonucleic acid)
106
Types of neutral lipids
- Waxes
- Oils
- Fats
- Saturated fats
- Unsaturated fats
107
Involve carbon chains that are saturated with hydrogen (liquid at room temp)
Saturated fats
108
Have carbon double bonds (semi-solid at room temp)
| Healthier
Unsaturated fats
109
In a marathon what saccharide do you want?
polysaccharide
110
If blood sugar is low, what saccharide do you want?
monosaccharide
111
10+ monosaccharides joined by chemical bond
Cellulose - plant cell wall
Chitin - bug exoskeleton
Polysaccharide
112
2 monosaccharides joined by chemical bond
| Some disaccharides are joined by glycosidic bonds
Disaccharides
113
made by 2 molecules in alpha position and joined by O2
Glycosidic bond
114
Made of 1 type of sugar
Usually has 3-7 carbons: triose, pentose, hexose
Can occur in line or fold in rings
Monosaccharide
115
If a monosaccharide is linear, how do you count it?
Top to bottom
116
If a monosaccharide is in rings, how do you count it?
Start at the 3:00 position and count clockwise
117
If OH is below first Carbon, it is in ___ position
Alpha
118
If OH is above first Carbon, it is in ___ position
Beta
119
Sugar
Ends in "ose"
gives you energy
Carbohydrates
120
2 or more molecules with same chemical formula, but different molecular structures
Isomer
121
if isomers are mirror images of another
"L Isomer" = left
"D Isomer" = right
Stereoisomer
122
If components of water are removed in a chemical reaction
| Used when building more complex molecule
Dehydration reaction
123
If components of water are added in chemical reaction
| Used when breaking down molecules
Hydrolysis reaction
124
Many units bound together ; when hydration is used, we make them
Polymer
125
Individual subunit; when hydrolysis is used, we make them
Monomer
126
4 main biological molecules:
Carbohydrates
Lipids
Proteins
Nucleotides/nucleic acids
127
2 molecules with same chemical formula but components are attached different ways
structural isomer
128
taking an unsaturated fat and bombarding it with hydrogen to make it more saturated
longer shelf life and food less greasy
hydrogenation
129
Groups include P
Component in DNA
Molecules donate phosphate to give energy
Phosphate
130
Groups include S
| Skunk Spray
sulfhydryl
131
Hydrophobic
Partially or entirely non polar
neutral, phospholipids, and steriods
Lipids
132
Enzymes speed up chemical reactions by lowering the ____
activation energy
133
Substance that an enzyme is acting upon
Substrate
134
Most enzymes end in "___"
"ase"
135
Sign on an enzyme that binds to the substrate (Indention in enzyme)
Active sight
136
When enzyme changes its shape slightly so it has a more perfect and tight hold on the substrate
Induced fit
137
How does an enzyme break easier and quicker?
It stresses the bonds forcing it to break
138
Catalysts & do the same job as enzymes, but they are not proteins
ribozymes
139
Rate that enzymes are speeding up reactions
Rate of catalysis
140
Term when amount of substrates outnumber amount of enzymes
Saturated
141
3 main ways cells regulate enzyme activity:
1) competitive & noncompetitive inhibition
2) allosteric activation & allosteric inhibition
3) through chemical modification
142
The substrate and an inhibitor compete for the active site. Purpose is to stop it from activating too early
Competitive Inhibition
143
The inhibitor and substrate aren't competing over the active site. The inhibitor binds to a site other than active site, then induced fir occurs so the substrate cannot bind
Noncompetitive inhibition
144
Refers to a sit on enzyme other than active site; only way substrate can fit in the enzyme is when the activator binds to the allosteric site
Allosteric activation
145
when the inhibitor binds to allosteric site, the substrate can;t bind to active site so only one can bind at a time
Allosteric inhibition
146
Adding or taking something away to change the chemical structure in order to keep a chemical reaction from occurring or making a chemical reaction occur
Chemical modification
147
If ___ or ____ changes too much, it can kill an enzyme (homeostasis)
Temperature; pH
