Unit 1 Flashcards
1
Q
Living Organisms
A
Composed of common set of chemical components and similar structures
-depend on interactions among structurally complex parts to maintain the living state
-genetic information
-convert molecules
-extract energy from enviroment and use it for life
-replicate genetic information
-fundamental set of genes with structural similarities
-evolve through gradual genetic changes
2
Q
Three domains of life
A
Bacteria, archaea, eukarya= Luca(last universal common ancestor)
3
Q
Inductive biotic theory
A
Relate to mitchoandria and chloroplasts
4
Q
Inductive logic/reasoning:
A
Used to form hypothesis, specific to general
5
Q
Deductive logic/reasoning
A
Used to create testable predictions assuming hypothesis is supported, general to specific predictions
6
Q
In metabolism the action of going from subunits to macro units is called what?
A
Anabolism( ATP to ADP)
7
Q
Isotopes
A
Different number of neutrons, same number of protons
8
Q
Radioisotope:
A
Unstable and spontaneously breakdown going off energy, short life
9
Q
Unequal sharing of electrons happens when:
A
The two atoms are different elements- electronegativity difference
10
Q
Non polar bond
A
Electrons shared equally
11
Q
Polar bond
A
Electrons are pulled closer to the nucleus of the more electronegative atom
12
Q
A large difference in electronegativity results in what type of bond? Smaller difference?
A
Bigger= ionic, smaller= polar covalent
13
Q
In metabolism the action of going from macro units to subunits is called what
A
Catabolism (ADP to ATP)
14
Q
Ionic bonds tend to form what and that makes for what arrangement?
A
Crystals, anions and cation
15
Q
A characteristic of life is what
A
The ability to acquire and transform ENERGY from one form to another
16
Q
In general an anabolic reaction is what
A
Simple to complex molecules, energy INPUT is required(stored in chemical bonds)
17
Q
In general a catabolic reaction is:
A
Complex to simple, energy is released from chemical bonds
18
Q
Define Metabolism
A
The sum total of all chemical reactions occurring in a biological system at a given time
19
Q
Chemical reactions:
A
Involve energy changes, the energy in covalent bonds differed between the reactant and product.
20
Q
Any chemical reaction means there is a
A
Change in energy= transformation
21
Q
Energy
A
The capacity to do work
22
Q
Potentional energy
A
Energy stored in chemical bonds, concentration gradient, charge imbalance, etc.
23
Q
Kinetic energy
A
The energy of movement
24
Q
Types of energy in biology
A
Chemical(stored in bonds), electrical(separation of charges), heat(transfer due to temp. Difference) , light(electromagnetic radiation stored as photons), mechanical(energy of motion)
25
1st law of thermodynamics
Energy is neither created or destroyed, it can be converted
26
Second law of thermodynamics
When energy is converted from one form to another some of that energy become unavailable to do work (an example if heat)
27
Entropy definition
Some energy is converted to a non usable form associated with disorder and randomness- overall increasing in universe
28
The second law tells us:
A change that would decrease in entropy will not happen spontaneously- it will only happen is energy is added to system (ex: heating up water)
29
In a closed system the amount of usable energy will what with every transformation
Decrease
30
Total energy=
Usable(free) energy + unusable energy(entropy)
31
Only what type of energy can be used for cellular work
Free energy
32
Enthalpy(H)= free energy (G) + entropy(s)
33
A chemical reaction occurs when
Atoms combine or change their bonding partners
34
The ending -lysis means what
Breaking down something
35
If G is negative the reaction releases energy which is called what
Exergonic
36
If G is positive the reaction requires energy to occur which is called what
Endergonic
37
Chemical transformation require additional energy to initate the reaction is what
Activation Energy
38
Ea is required in what type of reactions
Endergonic and exergonic because covalent bonds in reactants must be broken first
39
Reaction rate is influenced by what
Activation energy, tempature, and concentration
40
Equilibrium
Rate of forward and reverse reaction are equal- relative concentrations of reactants and products will no longer change
41
Exergonic reactions:
Catabolic reations(complex to similar), complexity decreases and generates disorder, can occur spontaneously
42
Endergonic reactions
Consume free energy, include anabolic reactions(simple to complex), complexity(order) increases, localized decrease in entropy, not spontaneous
43
What bond in water makes it naturally cohesive
H bonding
44
The greater number of H bonds in liquid water gives it ? Specific heat
Higher
45
All hydrophilic (ionic, polar) molecules are?
Soluble (able to dissolve) in water
46
When acids dissolve in water they ? With H+
Release
47
A strong acid? A weak acid?
Dissociated completely in water, I complete dissociation
48
A buffer
Helps maintain constant pH by absorbing or releasing H+ ions, is a weak acid and is corresponding base
49
Hydroxyl group
R-OH, polar, h bonds with water to help dissolve molecules, enables linkage to other molecules by condensation(opposite of hydrolysis)
50
Aldehyde Group
R-C=O and that C is C-H, the C=O group is very reactive. Important in building molecules and in energy-releasing reactions.
51
Keto Group
R-C(this C is also C=O)-R, the C=O is important in carbohydrates and in energy reactions
52
Carboxyl Group
R-C=O(and the C is C-OH) this is acidic. Ionizes in living tissues from -COO^-, and H+ Enters into condensation reaction by giving up -OH some carboxylic acids important in energy releasing reactions
53
Amino Group
R-N-H(N is bonded to another H) Basic, accepts H+ in living issues to form -NH3+, enters into condemnation reactions by giving up H+
54
Phosphate Group
R-O,P=O,O,O (P is in middle with one double bond to O and the rest single bonds) acidic, enters into condensation reations giving up OH, when bonded to another phosphate, hydrolysis release much energy
55
Sulfhyrdryl Group
R-SH by giving up H two -SH groups can reaction to form a disulfide bridge, stabilizing protein structure
56
When attached to a larger molecule, funcational groups give properties to larger molecule
Phosphate groups are highly polar, tend to interact with water. Addition of phosphate group can turn a hydrophobic, non polar molecule into a hydrophilic polar one
57
Macro molecules are Polymers- polymers are
Long chains of smaller molecules called monomers joined by covalent bonds
58
Different polymer types are defined by the functional group that attaches to the
Carbon skeleton
59
Amino acids
Proteins
60
Nucleotides
Nucleic acid
61
Sugar
Polysaccharide (carbohydrates)
62
Phospholipid
Membrane (NOT A POLYMER- NOT Covalent bonds, but VAN DER Walls bonds)
63
Make a polymer by
Condensation (water out, energy in) AKA dehydration synthesis
64
Carbohydrates
-each carbon is being hydrated
65
General formula for carbohydrates
Cn(H2O)n
66
Types of carbohydrates/polysaccharides
-Monosaccharides
-disaccharides
-oligosacchrides
-polysaccharides
67
Monosaccharide
Smaller sugars- 3 to 6 carbons
68
Disaccharides
Two monosaccharides linked by covalent bonds
69
Oligosacchrides
3-20 monosaccharide’s
70
Polysaccharides
Hundreds or thousands of monosaccharide’s- starches, glycogen, cellulose
71
Glucose
Aldehyde groups at carbon 1
72
Alpha carbon ring
H on top of carbon 1
73
Beta Carbon ring/ glucose
H on Bottom
74
How to count Carbons
C1 is at the center of the C hole
75
Be able to name and identify Alpha, Beta, Glucose, Fructose, and Sucrose and others on slide 8 of lecture 4
76
Linear, branched, and highly branched examples
Cellulose, Strachey, glycogen
77
Highly branched molecules will have what type of energy
A lot of stored energy
78
Functions of Carbohydrates
-Cell energy: immediate- glucose adn other monosaccharide’s
- Cell energy: stored energy source- starch, glycogen
-Carbon Skeltons for many other molecules : sugar component of nucleotides- ribose, deoxyribose
-Cell recognition signals: attached to proteins or lipids on cell surface
-extracellular structures: cell walls (bacteria, plants, fungi), exoskeletons, cartilage
79
Nucleic acids: building block and function
Building block: nucleotides, the acids carry genetic information
80
DNA to DNA
Replication
81
DNA to RNA
Transcription
82
RNA to Polypeptide(protein)
Translation (think poLypeptide and transLation)
83
Neculeotides
The monomer, can be joined in chains or reversible attached to ther types of cell molecules (proteins)
84
Nucleic acids
Polymers of nucleotides, DNA= deoxyribonucleic acid, RNA= ribonucleic acid
85
Nucleic acid bases
Pyrimidines and Purines
86
Purines have
A and G, PURe As Gold
87
nucleotides=
Pentode sugar + phosphate group + nitrogenous base
88
Pyrimidines
C, T, U. (Think pyramids CUT)
89
The difference in the base of RNA and DNA is
DNA does not have OH at carbon 2, RNA does have OH at carbon 2
90
The bases interact at carbons:
carbon 3 of molecule one interacts with carbon 5 of molecule 2
91
When base paring in DNA and RNA the stands should be….
Going opposite ways (one is 3-5 carbons and the other 5-3 carbon) Unparallel
92
A goes with and G goes with
T and C (think AT and G and C make Great Complements)
93
Nucleotides are joined by what type of bond
Strong covalent bonds
94
Paired chains are bonded by what type of bond
Hydrogen Bond
95
A and T have how many H bonds
2 H bonds
96
G and C have how many hydrogen bonds
3 (think G and C are Great Complements- longer phrase= more hydrogen bonds)
97
RNA folds
A strand of RNA can also from intramolecular base pair bonds with itself folding to make a more complex double stranded shapes
98
DNA is always Double stands
99
Functions of DNA
-carries information for all of an organism’s structures and functions, held in specific sequence of base pairs
-can reproduce itself (replication using complementary base pairing)
-can copy specific segments of the information into RNA (transscRiption)
100
RNA can specify. Sequence of amino acids in a polypeptide
Structural and functional characteristics of cells
101
Functions for nucleotides
ATP- energy transducer in biochemical reactions (can go to ADP and AMP)
GTP- energy source in protein synthesis
cyclic AMP- essential to the action of hormones and transmission of information in the nervous system
102
Types of proteins
Enzymes, structural, defensive, signaling, receptor, membrane transporters, storage, transportation, gene regulation
103
Amino Acids are what type of bond, called what
Covalent bond, called peptide bond, joined amino acids are polypeptides
104
Know the generic amino acid structure
C in middle, a R bond (side chain), H bond to C, COO- (carboxyl group) bonded to C and H3N+ (amino group) bonded to C
105
Charged amino acids
The charges side interacts with water or with ions of opposite charge- positive charge will have a + in the R group. Negative will have a - in the R group
106
Hyrophilic amino acids with polar but un charges side chains form hydrogen bonds
All have CH2 or CH3
107
Amino acids with non polar hydrophobic side chains all have
CH3, or CH2
108
Special Cases
Cysteine, Glycine, Proline
109
Cysteine
Can for a s-s bridge with another Cys
110
Glycine
Can fit through tight corners in a folded protein
111
Proline
Can cause a kink or turn in a folded protein- R group also bonded to H2N+ group
112
Proteins 4 levels of structure
Primary- linear sequence
Secondary- regular, repeated pattern in different regions of the Aa chain that arise from H bonding between AA
Tertiary- 3D shape arises from interactions (ionic, H bonds, or hyrodphobic) between R groups
Quaternary- association of two ro more polypeptides to form the functional proteins
113
The secondary term has what shapes
Beta pleated sheet and alpha helix
114
Tertiary level has what type of bonds
H bonds, disulfide bridges, van der waals interaction, and ionic bonds
This is when it starts forming specific shapes
115
Disulfide bridges
The terminal SH group of cysteine can react with another cysteine side chain to for a -s-s bond (VERY IMPORTANT IN PROTEIN FOLDING)
116
Enzymes are
Catalytic molecules
117
Tertiary structure
If a protein is heated the secondary and tertiary structure is broken down to the protein is said to be denatured- when cooled returns to normal tertiary structure, demonstrating that the information to specific protein shape is contained in its primary structure
118
Non covalent interactions between proteins
Environmental factors can destabilize a protein structure
-pH changes disrupt ionic bonds
- heat or high concentrations of polar molecule disrupts h bonds
-non polar substances- can disrupt folding of proteins that have many hydrophobic interactions
- high concentration of polar solutes can disrupt h bonding
119
How to read the P20 measurements
Top- 10s
Middle- 1s
Bottom- .1s
120
How to read P200 measurements
Top- 100s
Middle- 10s
Bottom- 1s
121
How to read P1000 measurements
Top- 1000s
Middle- 100s
Bottom- 10s
122
Be able to calculate a serial dilution and explain it
It is when the first tube gets a 1:1 ratio of solution and water then the second tube gets a 1:1 ratio of tube 1’s solution and water, and so on
123
Hypothesis vs theory-
Hypothesis: educated guess, can be tested (can never be proven true
Theory: backed up by an idea, can be changed/revised
124
Homeostasis
Maintain consistent conditions in the cell
125
Dry lab 1 observations with salt water and leaf
When the leaf was with regular water it had chloroplasts all throughout the cell, when in salt water the chloroplasts collected, the membranes made a “line” , there was salt water inside the cell in the “open” area.
126
When cell membranes move away from the cell wall that shows what
Hypertonic
127
The outside of the cell with salt water is hypertonic to the cytoplasm therfore
Water wants to move out
128
The fresh water and cell was hypotonic to the outside in freshwater to cytoplasm
The cytoplasm was hypertonic to water
129
Plasmolysis:
The movement of water from the cell into the environment causing the plasma membrane to pull away from the cell wall. In hypertonic conditions the cell is prevented from bursting due to presence of elastic but rigid cell walls.
130
Osmosis
The movement of water from LOW solute concentration (hypotonic) to HIGH concentration (hypertonic) via permeable membrane (plasma membrane)
131
Hypertonic
High concentration solution
132
Hypotonic
Low concentration solution
133
Isotonic
The balance of concentration solutions (equal)
134
Negative control
Should have no change from adding something, control for false positives
135
Positive control
Expected outcome/desired outcome- adding something you know works. Controls for false negatives
136
Dependent vs independent variables
Dependent- variable being measured in output
Independent- variable the gets manipulated
137
Polymers
Most macromolecules are made of this, they are long chains of smaller molecules called monomers, joined covalently
138
Building blocks of life:
Amino acids- proteins, nucleotides- Nucleic acid, sugar-polysaccharide (all are polymers)
Phospholipid- membrane (not a polymer, not covalently bonded
139
How to make a polymer
Dehydration synthesis- an H2O group leaves so that the monomer can attach with the other monomer
140
How to break a polymer
Hydrolysis- (water in, energy out) where a monomer will break with another monomer H2O will go in, the OH attaching to the monomer and the H attaching to the polymer
141
Carbohydrates/polysaccharides
General formula of C_n(H2)_n, includes small sugars and long polymers of sugars, there are 4 categories: monosaccharide, disaccharide, oligosacchrides, and polysaccharide
142
Monosaccharides
Smallest sugar- 3C to 6C
143
Disaccharides
Two monosaccharide’s link by covalent bonding
144
Oligosacchrides
3-20 monosaccharides
145
Polysaccharides
Hundreds or thousands of monosaccharides- starch, glycogen, cellulose
