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BIOL 1101 > Lecture 1: Foundations Of Biology > Flashcards

Lecture 1: Foundations Of Biology Flashcards

1
Q

Scientific method

A

Making observations, developing explanations and testing those explanations

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2
Q

What must a hypothesis be

A

Falsifiable and testable (falsifiable meaning the ability to be proven false)

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3
Q

Failure to falsify a hypothesis means the hypothesis is true

A

Wrong - there still must be data to prove its validity

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4
Q

Variables in an experiment

A

Independent- changed by scientist
Dependent- response to changes in independent variables
Controlled- remains constant

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5
Q

Experimental vs Observational science

A

Observational- infer a pattern and cause for collected data, and use statistical techniques

Experiment: data collected through controlled experiments

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6
Q

Organization of matter (matter, element, and compound)

A

matter- has mass and occupies space (Consisting of pure elements)
Element- cant be broken down to other substances by chemical reactions
Compound- two or more elements in a fixed ratio

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7
Q

Which elements make up 96% of the matter in living organisms

A
  • Carbon
  • Oxygen
  • Hydrogen
  • Nitrogen
    The ratios make living organisms different
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8
Q

Isotopes

A
  • same number of p+, different number of neutrons therefore different atomic mass but same atomic number
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9
Q

Radioisotopes

A

Unstable isotopes that decay and release energy, rate of their decay is constant

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10
Q

Radioactive tracers

A
  • substance containing a radioisotope that’s used to measure the speed of chemical processes or the movement of a substance

ex. used in imaging tests

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11
Q

Inert

A
  • elements with full valence shells
  • unreactive
  • ex. Neon
    Don’t form chemical bonds
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12
Q

Unequal sharing of electrons forms

A

a polar covalent bond, if hydrogen is one of the atoms= hydrogen bonding

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13
Q

Hydrogen bonding

A
  • partial positive H attracted to partial negative charge of nearby atoms
  • weaker than covalent and ionic bonds
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14
Q

Van der Waals forces

A
  • weaker than hydrogen bonds
  • develop between non polar molecules
  • constant motion of electrons causes them to accumulate creating zones of positive and negative charges (temporary)
  • polar molecules
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15
Q

ORDERING THE STRENGTH OF BOND TYPES

A

Ionic (strongest)
Covalent
Hydrogen
LDF

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16
Q

Inter vs intra

A

Inter- between
Intra- within

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17
Q

Hydrogen bonds and water

A

More dense- liquid form: dynamic (movement) can be used in living cells

Less dense- solid form: ice
- stable, rigid lattice structure prevent it from being used in cells

  • ice rigid lattice structures expand and form crystals that can puncture and disrupt cell membranes
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18
Q

Characteristics of water

A
  • high specific heat capacity allows water to stay liquid between 0-100 degrees Celsius
  • attraction between water molecules cause cohesion
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19
Q

Why is cohesion important for plants

A
  • keeps water molecules connected, allowing them to move agains the force of gravity easily
  • whenever water evaporates, stomata pull water to stems from roots
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20
Q

Hydration shell

A
  • water molecules surround polar molecules and ions
  • allows for the separation of molecules until it reaches a saturation point
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21
Q

Buffers

A
  • controls pH, allowing it to stay neutral
  • absorbs or releases protons

IN OUR BLOOD:
- kidneys regulate pH by excreting acids in urine
- produce and regulate Bicarbonate to increase pH

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22
Q

Living matter are composed of carbon compounds

A

Making them organic

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23
Q

Synthesis of a polymer

A

synthesis of a polymer:
- dehydration synthesis reaction
- remove water
- form a bond

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24
Q

Breakdown of a polymer

A

hydrolysis reaction:
- add water
- break a bond
- split water molecules

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25
carbohydrates
- sugars and the polymers of sugars - fuel for cells - building material (build various cellular components)
26
monosaccharides
- multiples of CH2O (1:2:1)
27
isomers of monosaccharides
- same chemical formula - different molecules structure, different function
28
mirror imaged isomers
Enantiomers - structural isomers - different position of carbonyl group
29
Disaccharides
- two monosaccharides - form a covalent bond: GLYCOSIDIC LINKAGE Glucose+Glucose=Maltose Glucose+Fructose=Sucrose Glucose+Galactose=Lactose
30
Polysaccharides
Branched: alpha glucose (from glycogen and starch) Unbranched: beta glucose (building) - form different glycosidic linkages: H bonds and N groups
31
Proteins
MADE UP OF POLYPEPTIDES - various structures, various functions - structural support, storage, transport, etc. - 100 000 different human proteins (transcription and translation are the blueprint to build these proteins)
32
polypeptides
polymers of amino acids
33
how many different types of amino acids
- 20 different amino acids made unique based on their R group central carbon= alpha carbon N terminus (amino group) C terminus (carboxyl group) also have a functional group attached
34
What are the non polar amino acids
Glycine (Gly, G) Alanine (Ala, A) Valine (Val, V) Leucine (Leu, L) Isoleucine (Ile, I) Methionine (Met, M) Proline (Pro, P) Cysteine (Cys, C) *pH of environment can affect its polarity** Phenylalanine (Phe, F) Tryptophan (Trp, W) GREAT ARTISTS VALUE LIFE, IN MY PRETTY CRAZY PAINTING TIME
35
What are the uncharged polar amino acids (partial charge)
Serine (Ser, S) Threonine (Thr, T) Asparagine (Asn, N) Glutamine (Gln, Q) Tyrosine (Tyr, Y) STAG-T
36
Acidic (negative charge) polar amino acids
Aspartic acid (Asp, D) Glutamic acid (Glu, E) AG (2 letters=even, think opposite so odd=negative)
37
Basic (positive charge) polar amino acids
Lysine (Lys, K) Arginine (Arg, R) Histidine (His, H) LAH (3 letters=odd, think opposite so even=positive)
38
Peptides
- covalent bond - formed by dehydration synthesis - amino acid added only to carboxyl end = Peptide Bond, connect together in a polypeptide bond amino acids are joined by peptide bonds to form PEPTIDES (by linking carboxyl ends) then they will form POLYPEPTIDE CHAINS through peptide bonds which are the building block of protein structure
39
Primary Protein Structure
1)- linear sequence of amino acids tells us nothing about its structure N-terminus .... Amino acid sequence.... C-terminus
40
Secondary Protein Structure
H bonds between amino acids as part of backbone to connect both strands - O and H of backbone folds - forms either an alpha helix or Beta pleated sheet
41
Primary and secondary protein structures only
involve bonds between amino and carboxyl groups
42
Tertiary protein structure
- all types of bonds between R groups - will form chemical bonds with each other - 3D Shape - Function - no bond formation and non polar behaviour leads to hydrophobic interactions
43
Quaternary Protein structure
less than or equal to 2 polypeptides - all types of bonds Hemoglobin For Example needs 4 polypeptides
44
Prosthetic groups
- part of quaternary protein structure - non-protein molecules/compounds added to protein after to allow for function ex. Heme
45
Heme as a prosthetic group
- helps hemoglobin bind and deliver O2 - iron core - essential for the function of hemoglobin
46
Nucleic acids
- polymers of nucleotides - genetic information=inheritance 1) DNA 2) RNA a) mRNA (messenger) b) tRNA (transfer) c) rRNA (ribosomal)
47
nucleotides
3 parts (covalent bonds) 1) nitrogenous base 2) pentose sugar 3) 1-3 phosphate groups
48
difference between DNA and RNA
- if carbon 2 in the nucleotides contain OH or H OH-RNA H- DNA
49
A) Which nucleotide is only found in RNA B) Which nucleotide is only found in DNA C) Which nucleotide are used in energy transfer
a) URACIL b) THYMINE c) ADENINE AND GUANINE
50
Pyrimidines vs Purines
Pyrimidines- 1 carbon ring Purine- 2 carbon rings
51
DNA and RNA structure
- 2 nucleotide chains - sugar phosphate backbone - phosphodiester bonds (building nucleic acids) - nitrogenous bases inside - H bonds
52
How is DNA read
from 5 to 3
53
DNA structure
- PO4 and sugar backbone - Nitrogenous bases are NOT part of backbone - Use nitrogenous bases to form H bonds between 2 strands of polynucleotides to form double strands
54
Anti parallel strands
5-3 3-5 complementary strands that run in opposite direction + knowing the sequence of one DNA strand means you can predict the other 3 C-G 2 A-T
55
RNA structure
- Single stranded - no hydrogen bond formation between nitrogenous bases
56
Lipids
- non polar molecule: hydrocarbon backbone - not a true macromolecule=no defined monomer subunit - biological lipids: fat, phospholipids, steroids
57
Fatty acids
Saturated: - maximum number of hydrogen atoms - linear: no double bonds - increased density: can be packed in - room temp=solid ex. butter, stearic acid Unsaturated: - one or more double bonds - room temperature=liquid - decreased density, pockets of air - ex. oleic acid triglycerides= 3 fatty acid chain - formed through dehydration synthesis
58
What has more energy: 1g of starch or 1g of fat
1g of fat: holds more energy in fatty acid chains C-H bonds store more energy
59
phospholipids
- major lipid found in membranes - amphipathic: polar and non polar components
60
steroids
- form of lipid: isoprene backbone - 4 carbon ring - dual solubility: np and p ends
61
cells
composed of major macromolecules - structural organization will impact function
62
All macromolecules
- proteins - nucleic acids - carbs - lipids
63
differentiate between nitrogenous bases nucleic acids and nucleotides with regards to the formation of DNA
Nitrogenous bases (a,c,t,g) pair via hydrogen bonds to stabilize the double helix structure of DNA, while nucleotides (sugar, PO4, and base) link together through phosphodiester bonds to form the sugar-phosphate backbone of nucleic acids (DNA, RNA)

BIOL 1101 (18 decks)

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