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Unit 1 Flashcards

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Biology 101 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

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2
Q

Three domains of life

A

Bacteria, archaea, eukarya= Luca(last universal common ancestor)

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3
Q

Inductive biotic theory

A

Relate to mitchoandria and chloroplasts

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4
Q

Inductive logic/reasoning:

A

Used to form hypothesis, specific to general

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5
Q

Deductive logic/reasoning

A

Used to create testable predictions assuming hypothesis is supported, general to specific predictions

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6
Q

In metabolism the action of going from subunits to macro units is called what?

A

Anabolism( ATP to ADP)

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7
Q

Isotopes

A

Different number of neutrons, same number of protons

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8
Q

Radioisotope:

A

Unstable and spontaneously breakdown going off energy, short life

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9
Q

Unequal sharing of electrons happens when:

A

The two atoms are different elements- electronegativity difference

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10
Q

Non polar bond

A

Electrons shared equally

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11
Q

Polar bond

A

Electrons are pulled closer to the nucleus of the more electronegative atom

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12
Q

A large difference in electronegativity results in what type of bond? Smaller difference?

A

Bigger= ionic, smaller= polar covalent

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13
Q

In metabolism the action of going from macro units to subunits is called what

A

Catabolism (ADP to ATP)

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14
Q

Ionic bonds tend to form what and that makes for what arrangement?

A

Crystals, anions and cation

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15
Q

A characteristic of life is what

A

The ability to acquire and transform ENERGY from one form to another

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16
Q

In general an anabolic reaction is what

A

Simple to complex molecules, energy INPUT is required(stored in chemical bonds)

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17
Q

In general a catabolic reaction is:

A

Complex to simple, energy is released from chemical bonds

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18
Q

Define Metabolism

A

The sum total of all chemical reactions occurring in a biological system at a given time

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19
Q

Chemical reactions:

A

Involve energy changes, the energy in covalent bonds differed between the reactant and product.

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20
Q

Any chemical reaction means there is a

A

Change in energy= transformation

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21
Q

Energy

A

The capacity to do work

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22
Q

Potentional energy

A

Energy stored in chemical bonds, concentration gradient, charge imbalance, etc.

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23
Q

Kinetic energy

A

The energy of movement

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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)

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25
Q

1st law of thermodynamics

A

Energy is neither created or destroyed, it can be converted

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26
Q

Second law of thermodynamics

A

When energy is converted from one form to another some of that energy become unavailable to do work (an example if heat)

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27
Q

Entropy definition

A

Some energy is converted to a non usable form associated with disorder and randomness- overall increasing in universe

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28
Q

The second law tells us:

A

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)

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29
Q

In a closed system the amount of usable energy will what with every transformation

A

Decrease

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30
Q

Total energy=

A

Usable(free) energy + unusable energy(entropy)

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31
Q

Only what type of energy can be used for cellular work

A

Free energy

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32
Q

Enthalpy(H)= free energy (G) + entropy(s)

A
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33
Q

A chemical reaction occurs when

A

Atoms combine or change their bonding partners

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34
Q

The ending -lysis means what

A

Breaking down something

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35
Q

If G is negative the reaction releases energy which is called what

A

Exergonic

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36
Q

If G is positive the reaction requires energy to occur which is called what

A

Endergonic

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37
Q

Chemical transformation require additional energy to initate the reaction is what

A

Activation Energy

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38
Q

Ea is required in what type of reactions

A

Endergonic and exergonic because covalent bonds in reactants must be broken first

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39
Q

Reaction rate is influenced by what

A

Activation energy, tempature, and concentration

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40
Q

Equilibrium

A

Rate of forward and reverse reaction are equal- relative concentrations of reactants and products will no longer change

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41
Q

Exergonic reactions:

A

Catabolic reations(complex to similar), complexity decreases and generates disorder, can occur spontaneously

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42
Q

Endergonic reactions

A

Consume free energy, include anabolic reactions(simple to complex), complexity(order) increases, localized decrease in entropy, not spontaneous

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43
Q

What bond in water makes it naturally cohesive

A

H bonding

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44
Q

The greater number of H bonds in liquid water gives it ? Specific heat

A

Higher

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45
Q

All hydrophilic (ionic, polar) molecules are?

A

Soluble (able to dissolve) in water

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46
Q

When acids dissolve in water they ? With H+

A

Release

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47
Q

A strong acid? A weak acid?

A

Dissociated completely in water, I complete dissociation

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48
Q

A buffer

A

Helps maintain constant pH by absorbing or releasing H+ ions, is a weak acid and is corresponding base

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49
Q

Hydroxyl group

A

R-OH, polar, h bonds with water to help dissolve molecules, enables linkage to other molecules by condensation(opposite of hydrolysis)

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50
Q

Aldehyde Group

A

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.

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51
Q

Keto Group

A

R-C(this C is also C=O)-R, the C=O is important in carbohydrates and in energy reactions

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52
Q

Carboxyl Group

A

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

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53
Q

Amino Group

A

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+

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54
Q

Phosphate Group

A

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

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55
Q

Sulfhyrdryl Group

A

R-SH by giving up H two -SH groups can reaction to form a disulfide bridge, stabilizing protein structure

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56
Q

When attached to a larger molecule, funcational groups give properties to larger molecule

A

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

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57
Q

Macro molecules are Polymers- polymers are

A

Long chains of smaller molecules called monomers joined by covalent bonds

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58
Q

Different polymer types are defined by the functional group that attaches to the

A

Carbon skeleton

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59
Q

Amino acids

A

Proteins

60
Q

Nucleotides

A

Nucleic acid

61
Q

Sugar

A

Polysaccharide (carbohydrates)

62
Q

Phospholipid

A

Membrane (NOT A POLYMER- NOT Covalent bonds, but VAN DER Walls bonds)

63
Q

Make a polymer by

A

Condensation (water out, energy in) AKA dehydration synthesis

64
Q

Carbohydrates

A

-each carbon is being hydrated

65
Q

General formula for carbohydrates

A

Cn(H2O)n

66
Q

Types of carbohydrates/polysaccharides

A

-Monosaccharides
-disaccharides
-oligosacchrides
-polysaccharides

67
Q

Monosaccharide

A

Smaller sugars- 3 to 6 carbons

68
Q

Disaccharides

A

Two monosaccharides linked by covalent bonds

69
Q

Oligosacchrides

A

3-20 monosaccharide’s

70
Q

Polysaccharides

A

Hundreds or thousands of monosaccharide’s- starches, glycogen, cellulose

71
Q

Glucose

A

Aldehyde groups at carbon 1

72
Q

Alpha carbon ring

A

H on top of carbon 1

73
Q

Beta Carbon ring/ glucose

A

H on Bottom

74
Q

How to count Carbons

A

C1 is at the center of the C hole

75
Q

Be able to name and identify Alpha, Beta, Glucose, Fructose, and Sucrose and others on slide 8 of lecture 4

A
76
Q

Linear, branched, and highly branched examples

A

Cellulose, Strachey, glycogen

77
Q

Highly branched molecules will have what type of energy

A

A lot of stored energy

78
Q

Functions of Carbohydrates

A

-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
Q

Nucleic acids: building block and function

A

Building block: nucleotides, the acids carry genetic information

80
Q

DNA to DNA

A

Replication

81
Q

DNA to RNA

A

Transcription

82
Q

RNA to Polypeptide(protein)

A

Translation (think poLypeptide and transLation)

83
Q

Neculeotides

A

The monomer, can be joined in chains or reversible attached to ther types of cell molecules (proteins)

84
Q

Nucleic acids

A

Polymers of nucleotides, DNA= deoxyribonucleic acid, RNA= ribonucleic acid

85
Q

Nucleic acid bases

A

Pyrimidines and Purines

86
Q

Purines have

A

A and G, PURe As Gold

87
Q

nucleotides=

A

Pentode sugar + phosphate group + nitrogenous base

88
Q

Pyrimidines

A

C, T, U. (Think pyramids CUT)

89
Q

The difference in the base of RNA and DNA is

A

DNA does not have OH at carbon 2, RNA does have OH at carbon 2

90
Q

The bases interact at carbons:

A

carbon 3 of molecule one interacts with carbon 5 of molecule 2

91
Q

When base paring in DNA and RNA the stands should be….

A

Going opposite ways (one is 3-5 carbons and the other 5-3 carbon) Unparallel

92
Q

A goes with and G goes with

A

T and C (think AT and G and C make Great Complements)

93
Q

Nucleotides are joined by what type of bond

A

Strong covalent bonds

94
Q

Paired chains are bonded by what type of bond

A

Hydrogen Bond

95
Q

A and T have how many H bonds

A

2 H bonds

96
Q

G and C have how many hydrogen bonds

A

3 (think G and C are Great Complements- longer phrase= more hydrogen bonds)

97
Q

RNA folds

A

A strand of RNA can also from intramolecular base pair bonds with itself folding to make a more complex double stranded shapes

98
Q

DNA is always Double stands

A
99
Q

Functions of DNA

A

-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
Q

RNA can specify. Sequence of amino acids in a polypeptide

A

Structural and functional characteristics of cells

101
Q

Functions for nucleotides

A

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
Q

Types of proteins

A

Enzymes, structural, defensive, signaling, receptor, membrane transporters, storage, transportation, gene regulation

103
Q

Amino Acids are what type of bond, called what

A

Covalent bond, called peptide bond, joined amino acids are polypeptides

104
Q

Know the generic amino acid structure

A

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
Q

Charged amino acids

A

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
Q

Hyrophilic amino acids with polar but un charges side chains form hydrogen bonds

A

All have CH2 or CH3

107
Q

Amino acids with non polar hydrophobic side chains all have

A

CH3, or CH2

108
Q

Special Cases

A

Cysteine, Glycine, Proline

109
Q

Cysteine

A

Can for a s-s bridge with another Cys

110
Q

Glycine

A

Can fit through tight corners in a folded protein

111
Q

Proline

A

Can cause a kink or turn in a folded protein- R group also bonded to H2N+ group

112
Q

Proteins 4 levels of structure

A

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
Q

The secondary term has what shapes

A

Beta pleated sheet and alpha helix

114
Q

Tertiary level has what type of bonds

A

H bonds, disulfide bridges, van der waals interaction, and ionic bonds

This is when it starts forming specific shapes

115
Q

Disulfide bridges

A

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
Q

Enzymes are

A

Catalytic molecules

117
Q

Tertiary structure

A

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
Q

Non covalent interactions between proteins

A

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
Q

How to read the P20 measurements

A

Top- 10s
Middle- 1s
Bottom- .1s

120
Q

How to read P200 measurements

A

Top- 100s
Middle- 10s
Bottom- 1s

121
Q

How to read P1000 measurements

A

Top- 1000s
Middle- 100s
Bottom- 10s

122
Q

Be able to calculate a serial dilution and explain it

A

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
Q

Hypothesis vs theory-

A

Hypothesis: educated guess, can be tested (can never be proven true
Theory: backed up by an idea, can be changed/revised

124
Q

Homeostasis

A

Maintain consistent conditions in the cell

125
Q

Dry lab 1 observations with salt water and leaf

A

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
Q

When cell membranes move away from the cell wall that shows what

A

Hypertonic

127
Q

The outside of the cell with salt water is hypertonic to the cytoplasm therfore

A

Water wants to move out

128
Q

The fresh water and cell was hypotonic to the outside in freshwater to cytoplasm

A

The cytoplasm was hypertonic to water

129
Q

Plasmolysis:

A

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
Q

Osmosis

A

The movement of water from LOW solute concentration (hypotonic) to HIGH concentration (hypertonic) via permeable membrane (plasma membrane)

131
Q

Hypertonic

A

High concentration solution

132
Q

Hypotonic

A

Low concentration solution

133
Q

Isotonic

A

The balance of concentration solutions (equal)

134
Q

Negative control

A

Should have no change from adding something, control for false positives

135
Q

Positive control

A

Expected outcome/desired outcome- adding something you know works. Controls for false negatives

136
Q

Dependent vs independent variables

A

Dependent- variable being measured in output
Independent- variable the gets manipulated

137
Q

Polymers

A

Most macromolecules are made of this, they are long chains of smaller molecules called monomers, joined covalently

138
Q

Building blocks of life:

A

Amino acids- proteins, nucleotides- Nucleic acid, sugar-polysaccharide (all are polymers)

Phospholipid- membrane (not a polymer, not covalently bonded

139
Q

How to make a polymer

A

Dehydration synthesis- an H2O group leaves so that the monomer can attach with the other monomer

140
Q

How to break a polymer

A

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
Q

Carbohydrates/polysaccharides

A

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
Q

Monosaccharides

A

Smallest sugar- 3C to 6C

143
Q

Disaccharides

A

Two monosaccharide’s link by covalent bonding

144
Q

Oligosacchrides

A

3-20 monosaccharides

145
Q

Polysaccharides

A

Hundreds or thousands of monosaccharides- starch, glycogen, cellulose

Bio (5 decks)

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