C5 Chemistry of Life Flashcards

(50 cards)

1
Q

organic vs inorganic

A
  • organic: carbon based compounds, larger and more complex
  • inorganic: not carbon based, simpler/smaller
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2
Q

organic chemistry

A

chemistry of carbon compounds within living things
- other important elements include: O2, H, N, P

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3
Q

State the 4 components essential for life.

A
  • water
  • minerals
  • vitamins
  • biomolecules
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4
Q

Describe how water is essential for life.

A
  • water makes up the greatest % of the body
  • universal solvent
  • an important medium for reactions
  • has a low viscosity = a transport medium (can move easily through small spaces/allow small substances to move through)
  • benefits to plants: support/rigour, adhesive + cohesive properties
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5
Q

Briefly outline what vitamins and minerals are, the two types, and how they are essential for life.

A
  • inorganic ions
  • make up many biomolecules
  • aid key biological processes

Macronutrients: elements needed in large quantities
Micronutrients: elements needed in small quantities
- not having enough = deficiencies

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6
Q

What are vitamins?
What are the two types

A

VITAMINS
- around 13 essential for health
- all except VD must be obtained externally (food)

TWO TYPES
- fat soluable (dissolves in fat)
- water soluable (dissolved in water)

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7
Q

polymers vs monomers

A
  • monomers: smaller molecules/building blocks
  • polymers: larger molecules, subcomponents of monomers
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8
Q

State the four categories of bio/macromolecules needed for life, and their corresponding monomer.

A
  • carbs (monosaccharides)
  • lipids (fatty acids + glycerol)
  • proteins (amino acids)
  • nucleic acids (nucleotides)
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9
Q

metabolism

A
  • the sum total of all enzyme-catalysed chemical reactions that occur within the body
  • includes catabolism and anabolism
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10
Q

catabolism vs anabolism

A

Catabolism
- decomposition
- polymers break down to monomers
- releases energy
- includes hydrolysis

Anabolism
- synthesis
- uses energy
- monomers built up to polymers
- includes condensation reactions

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11
Q

CARBS - biomolecule
- consist of… and their ratio
- monomers (…two? multiple?)

MONOMER
- what are they
- main functions (2)
- provide examples (2)

POLYMER
- main functions (2)
- provide examples (3)

A
  • Consist of: C, H, O (1:2:1 ratio)
  • Monomer: monosaccharides (2 = disaccharide)
  • Polymer: polysaccharide

MONOSACCHARIDES (monomer)
- single sugar molecules
Functions: an energy source for cell metabolism, structural component for polysaccharides
- glucose, ribose

POLYSACCHARIDES (polymer)
- Functions: energy storage, structural support for plants
- cellulose, starch, glycogen

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12
Q

glucose

A
  • monosaccharide
  • source of energy for CR (energy released helps ATP production)
  • produced by Phs
  • animals cannot make, must consume it (or break down polysaccharides)
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13
Q

ribose

A
  • monosaccharide
  • drives synthesis of RNA, DNA and ATP
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14
Q

cellulose

A

structural support in plant cells
- polysaccharide
- not easily broken down (humans cannot)

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15
Q

starch

A

glucose storage in plants
- polysaccharide
- found in seeds and plant roots
- easily broken down by enzymes

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16
Q

glycogen

A

SHORT term storage of sugar in animals
- polysaccharide
- if blood glucose levels drop, glycogen is broken down to release glucose for energy
- located in the liver + skeletal muscles

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17
Q

LIPIDS - biomolecule
- consist of… and their ratio
- monomers (2)
- key qualities (2)
- main functions (3)
- types (2)
- what is the polymer, and what does it consist of?

A
  • Consist of: C, H, O (no set ratio, but greater than 2:1 of H:O)
  • Monomers: fatty acids + glycerol
  • Qualities: hydrophobic, relatively insoluble
  • Functions: long term energy store, body insulation, aid micronutrient absorption
  • Two types: fats/waxes (solid room temp) + oils (liquids room temp)

TRIGLYCERIDES (polymer)
- Consist of: 1x glycerol, 3x FAC

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18
Q

saturated vs unsaturated fats

A
  • fats are a type of lipid

Saturated
- the fatty acid chains are saturated with H
- the greatest number of H possible
- no double bonds

Unsaturated
- one or more double bonds (look like bends/kinks in the fatty acid chain)

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19
Q

relative insolubility
- how lipids are important due to this (3)

A

Lipids are insoluble:
- fats are nonpolar (have no + or - regions)
- water is polar (has + and - regions)
- lipids attracted to lipids, H2O attracted to H2O = they never mix

Important role in:
- maintaining osmotic balance
- formation of cell membranes
- providing protective, hydrophobic coating (hair, skin, feathers, leaves)

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20
Q

essential fatty acids
- functions (3)
- example

A
  • essential to body, but we must ingest (cannot produce)
  • Functions: cell membrane structure, gene transcription, energy sources
  • e.g. omega-3
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21
Q

phospholipids
- what?
- consist of?
- qualities (2)
- main function

A
  • a specialised type of lipid (not true fats)
  • 1x glycerol, 2x FAC, 1x phosphate group
  • are amphipathic (hydrophilic head + hydrophobic tail)
22
Q

PROTEINS - biomolecule
- consist of?
- monomer
- polymer

MONOMER
- how many types?
- describe the structure
- describe how polymer is formed

PROTEIN STRUCTURE (4)
- describe

PROTEIN TYPES (2)
- describe
- functions
- examples

A
  • Consist of: C, H, O, N
  • Monomer: amino acids
  • Polymer: polypeptide chains

AMINO ACIDS
- 20 different types
Structure
- central C atom, attached to:
- R group
- carboxyl group (COOH)
- amino group (NH2)
- hydrogen atom (H)

  • AAs join together to form a dipeptide + H2O
  • this bond is called a peptide bond
  • multiple AAs binding together form a polypeptide chain (polymer)
  • these fold up to form proteins

PROTEIN STRUCTURE
- Primary: a linear sequence of AAs (a PP chain)
- Secondary: the PP chain twists into a repetitive structure (double helix)
- Tertiary: PP chain folds into a more complex, 3D shape
- Quaternary: multiple PP chains join together to form a protein

PROTEIN TYPES
Fibrous
- long narrow strands
- secondary structure
- Functions: support, structure, movement
- they ARE something (keratin in hair/nails, elastin in skin)

Globular
- compact + rounded
- tertiary structure
- Functions: controls/assists biological functions
- they DO something (haemoglobin, enzymes, antibodies)

23
Q

denaturing

A

a structural change in a protein that results in the loss of its biological properties
- AS of enzyme changes shape
- no longer compatible to specific substrate(s)
- reaction doesn’t occur

  • can be reversible or permanent
  • Caused by: temp, pH change, chemicals
24
Q

NUCLEIC ACIDS - biomolecule
- consist of?
- monomer
- polymers (2)

MONOMER
- made up of?
- describe structure

POLYMERS
- functions of each

A
  • Consist of: C, H, O, N, P
  • Monomer: nucelotides
  • Polymers: DNA + RNA

NUCLEOTIDES (monomer)
- Made up of: 5 carbon-pentose sugar (ribose/deoxyribose), phosphate group, nitrogenous base (A/G/C/T/U)
- sugar in middle, base + phosphate attached to either side

DNA/RNA (polymers)
- DNA function: carry/contain all genetic information in all cells
- RNA function: transfer specific genes outside the nucleus to synthesise proteins

25
Describe the 3 differences between DNA + RNA.
DNA - deoxyribose sugar - adenine, guanine, cytosine, thymine - double stranded RNA - ribose sugar - adenine, guanine, cytosine, uracil - single stranded
26
enzymes - what - structure
- biological catalyst (lower the activation energy for the body's chemical reactions - they facilitate, speed up + control reactions - not a reactant: are unchanged after reaction and can be used again STRUCTURE - globular proteins - many unique enzymes, each with a specific active site (AS) - AS of an enzyme has a specific complementary shape to a specific substrate (reactant)
27
Describe the model that best describes how enzymes bind to a substrate.
INDUCED FIT MODEL - can be either anabolic reactions or catabolic reactions 1. The substrate bonds to the enzyme's active site. 2. AS changes to become more complementary to the substrate, forming the enzyme-substrate complex (ESC) 3. The reaction occurs (anabolic/catabolic), products are released
28
Describe the two types of reaction that enzymes facilitate.
- Catabolic: polymers to monomers - Anabolic: monomers to polymers
29
Describe the factor affecting the rate of an enzyme-facilitated reaction.
TEMP - each enzyme has an optimum (37°C for humans) - Lower: slower ROR = less KE = less reactions - Higher: enzyme denatures (AS changes shape) - graph will increase to optimum, then rapidly decrease (denaturing) pH - each enzyme has an optimum pH depending on where it functions in the body (e.g. stomach = pH 2) - graph will increase to optimum, then rapidly decrease (denaturing) Substrate - substrate conc increases = ROR increases - limited by enzyme conc - graph will increase then plateau Enzyme - enzyme conc increases = ROR increases - limited by substrate conc - graph will increase then plateau
30
Describe the factors that assist or inhibit enzyme activity.
ASSISTING Cofactors - inorganic molecules that bond with the allosteric site of an enzyme - changes shape of the AS to be more complementary to the substrate Co-enzymes/co-substrates - organic molecules that bond with the AS - help substrate bond faster to enzyme INHIBITING Competitive - molecule bonds to the AS, preventing the substrate from bonding - reaction cannot occur Non-competitive - molecule bonds to the allosteric site, changing the shape of the AS - substrate cannot bond, reaction cannot occur
31
allosteric site
another site on an enzyme, seperate from the active site, that molecules are able to bond to - can be used for assisting or inhibiting enzyme activity
32
cellular respiration - what - word equation
the controlled release of energy from organic compounds (glucose, usually) in cells to form ATP - glucose + oxygen = carbon dioxide + water + ATP
33
ATP - what - structure - how does it work
Adenosine Triphosphate - type of nucleic acid: adenine base, ribose sugar, 3 phosphate groups - is a high energy molecule and an immediate power source for cell processes HOW - ATP releases energy via being hydrolysed (a cycle) - the third phosphate is held by an unstable bond, when it is released, it releases energy - results in ADP (Di) and Pi (the released phosphate) - ADP = low battery, energy used - can then be regenerated by adding Pi to form ATP again - ATP = full battery, energy ready to be released
34
anaerobic vs aerobic respiration - what - where - which occurs when?
ANAEROBIC - absence of O2 - partial breakdown of glucose - in the cytosol - small yield of ATP (2) from glycolysis AEROBIC - presence of O2 - complete breakdown of glucose - in the mitochondria - large yield of ATP (30-38) - aerobic is far more efficient - anaerobic is essential when the body is not able to get enough O2 to all cells (e.g. heavy exercise)
35
Outline/summarise the stages of cellular respiration (like a flow chart): - what occurs - where it occurs - net ATP yield
GLUCOSE | Glycolysis (cytoplasm) - 2 ATP | PYRUVATE | If O2 not present: Anaerobic CR (cytoplasm) - no more ATP produced - fermentation TOTAL: 2 ATP | If O2 present: Aerobic CR (mitochondria) - 30-34 ATP TOTAL: 30-38 ATP
36
CELLULAR RESPIRATION Describe the process of **glycolysis**: - where it occurs - when it occurs - total yield (products + ATP)
GLYCOLYSIS - in cytoplasm - starting process of both AN + AE resp Glucose is broken down into: - 2x pyruvate - 2x NADH (a co-enzyme needed for AE resp) - 2x ATP
37
CELLULAR RESPIRATION Describe the process of **AE** resp: - where it occurs - when it occurs - process steps - total yield (products + ATP)
AE RESP - in mitochondria - when O2 is present Process: - link reaction - Krebs cycle - electron transport chain Pyruvate converted to: - CO2 - H2O - (ideally) 34-36 ATP NET YIELD: 30-38 ATP (glycolysis + AE resp)
38
CELLULAR RESPIRATION Describe the process of **AN** resp: - where it occurs - when it occurs - fermentation (purpose, products and cycle process) - total yield (ATP)
AN RESP - in cytoplasm - when O2 is absent (body cannot get to cells fast enough) FERMENTATION Why - body cannot get O2 to cells fast enough, all stored ATP is used up, but energy is needed - AN resp restores NAD+ (needed in glycolysis reaction to convert to NADH) - the fermentation cycle allows glycolysis to continue to produce ATP in a low O2 environment Pyruvate (from glycolysis) converted to: - Animals: lactic acid (lactate) - Bacteria/yeast: ethanol + CO2 Process - is a reversible cycle - once O2 is present, lactic acid/ethanol is converted back to pyruvate - AE then continues as normal TOTAL YIELD: 2 ATP (glycolysis)
39
PHOTOSYNTHESIS - state equation - describe 2 stages: name, process, equation
- carbon dioxide + water = glucose + oxygen STAGE 1: Light Dependent - Process: photolysis - chlorophyll absorbs photon (light E) from the sun, excites H2O electrons, they become delocalised - chlorophyll takes an electron from H2O molecule, SPLITTING it into H2 (used in Stage 2), O2 (waste), + producing ATP - photon - chlorophyll - ATP + H2 (+ O2 waste) STAGE 2: Light Independent - Process: carbon fixation - H2 + ATP (from S1) + CO2 (from air) react to produce glucose
40
Describe the structure of the leaf referring to the important components (6).
- waxy cuticle: top + bottom of leaf - upper epidermis: transparent, allowing max light penetration for max Phs rate - palisade mesophyll: contains chloroplasts which contain chlorophyll, the main photosynthetic pigment - vascular bundle: xylem delivers H2O to cells for Phs, phloem transports glucose produced from Phs - spongy mesophyll: spaced out for gas exchange - stomata (pores): controlled by guard cells, facilitate GE (CO2 in, O2 out)
41
Describe ways of measuring the rate of Phs (directly/indirectly).
DIRECTLY - production of O2 (e.g. count bubbles produced by water plants) - uptake of CO2 (e.g. enviro pH increase) INDIRECTLY - increase in biomass (total mass of plant)
42
State the limiting factors of Phs and describe the shape of the graph when rate of Phs is on the Y axis.
TEMP - increase in temp = more KE = more frequent collisions = higher rate of Phs - graph has increase, then optimum, then decrease due to denaturing LIGHT INTENSITY - increase in light = more energy to drive reaction = higher Phs rate - graph will increase then plateau when chloroplasts are working at max efficiency CO2 CONC - increase in CO2 = more substrate = higher Phs rate - graph will increase then plateau due to another limiting factor
43
PHS VS CR - the reactions are complementary - products vs inputs - state equations for both - differences - similarities
- complementary reactions within the environment - products of Phs are inputs of CR, vice versa - PHS: CO2 + H2O = C6H12O6 + O2 - CR: O2 + C6H12O6 = H2O + CO2 DIFFERENCES - Phs: anabolic, synthesises/builds glucose - CR: catabolic, breaks down glucose - producers perform both, consumers perform just CR SIMILARITIES - both involve ATP production - Phs: ATP produced via light energy, used to make glucose - CR: ATP produced via breakdown of glucose - both require enzymes to complete the reaction
44
COMPENSATION POINT GRAPHS - what are they used to measure - what do they show - what is a comp point, when do they occur - what does above/below a comp point represent - describe how CR/Phs depends on time of day
- used to measure O2/glucose production, CO2/H2O use - demonstrates the relationship between CR + Phs (time of day/light on X axis, glucose/carb production on Y axis) - COMP POINT: when what is produced by Phs = what is used by CR (no excess), Phs rate = CR rate, usually occur at dusk/dawn - ABOVE CP: plant is producing more glucose then it is using - BELOW CP: plant is using more glucose than it is producing TIME OF DAY - rate of Phs is dependent (due to light availability) - highest rate is at midday - rate of CR is not dependent - rate remains relatively stable throughout day - goes up slightly when Phs increases, as needs small amount of ATP to start up
45
DNA - role of DNA - name complementary base pairs + bonds - sugar phosphate backbone structure + function - double helix: how is it formed REPLICATION - 2 stages, enzyme involved + process - the entire process is...
- Role of DNA: contains/carries all genetic information/genes for all cells - A + T (double H bond), G + C (triple H bond) BACKBONE - sugar phosphate backbone formed by the phosphates/sugars of nucleotides bonding to form a polynucleotide (polymer) - function: provide support + protection to N bases DOUBLE HELIX - caused by antiparallel strands (strands run in opposite directions) - causes twisting of strands to form an energy stable structure (the helix) - a fold occurs every 10-15 base pairs REPLICATION Stage 1 - Helicase enzyme moves along helix and unwinds DNA strands - each parent strand is a template for a new complementary daughter strand Stage 2 - DNA polymerase enzyme synthesises both new strands - the strands have complementary bases to parent strands - both stages happen at once - the process is semi-conservative (uses half of already formed material, half is created)
46
PROTEIN SYNTHESIS - why? - stages (2), their location, + process
WHY - DNA is too large and unstable to leave the nucleus - protein synthesis allows for singular genes to be transferred outside the nucleus, using mRNA, for a protein to be made TRANSCRIPTION - in nucleus - DNA is unwound at the location of the specific gene - a complementary strand of mRNA is made (U instead of T) - after it is formed, exits nucleus via a nuclear pore TRANSLATION - in cytoplasm - mRNA binds to a ribosome - ribosome translates mRNA one codon at a time - tRNA (transport) with complementary anti-codons (same as og DNA gene, but with U) drops off the specific AA that corresponds to the codon - the AAs bond together to form a PP chain - after entire mRNA strand is translated, the PP chain is formed
47
codon
3 bases, a set - code for a specific AA - translated together by a ribosome during protein synthesis
48
mRNA
messenger RNA - a smaller, more stable nucleic acid used to transfer specific genes outside the nucleus during protein synthesis
49
tRNA
transport RNA - a T shaped RNA molecule - has anticodons to the mRNA strand - brings a specific AA for each codon to form the PP chain
50
GENE (POINT) MUTATIONS - define - ways they can occur (4) - types of effects (4) - define degenerate
- a change in a single nucleotide in the DNA code, leading to a gene mutation WAYS - Substitution: base is replaced with a different one (ATG to ACG) - Inversion: two bases next to each other swap places (ATG to AGT) - Insertion: base is added in - Deletion: base is deleted EFFECTS - Missense mutation: mutation alters a single AA, leading to genetic variation, not always bad - Nonsense mutation: mutation causes a premature stop codon, PP chain is incomplete and dysfunctional, usually bad - Frameshift mutation: insertion/deletion shifts the entire DNA strand, PP chain is dysfunctional, usually very bad - Silent mutation: base changes but still codes for correct AA, no effect (this is possible as the DNA code = degenerate: alternate substances can perform the same function)