SBI4U - Unit 1: Biochemistry

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Last updated 12:59 AM on 9/23/25
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38 Terms

1
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Isotopes — how are they different from a normal atom? Uses? (2)

  • Atoms = neutral; ions = charged

  • Isotopes = same element, different neutrons.

    • Radioisotopes used in medicine

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Intramolecular bonds: Ionic bonds

what is it? how do they form? solubility? (3)

  • metal + nonmetal

  • transfer electrons

  • soluble in water.

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Intramolecular bonds: covalent bonds

what is it? how do they form?

  • nonmetals

  • share electrons

  • Can be polar (unequal sharing, dipoles) or nonpolar (equal sharing).

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intermolecular forces:

LDF

  • temporary & changing attraction b/w p+ & e- due to movement of electrons

  • found in all molecules

  • the bigger the molecule/more electrons, the stronger the LDFs

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intermolecular forces:

dipole-dipole

  • permanent attraction forces between POLAR molecules

  • partial + portion of 1 molecule is attracted to the partially - portion of another molecule

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intermolecular forces:

H-bonds

  • the strongest IMF

  • between H and N, O, or F

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how to determine if a covalent bond is non polar, polar or ionic-like covalent

  • determined by electronegativity difference

  • non polar covalent bond: 0.4 or lower

  • polar covalent bond: 0.4 < x < 1.7

  • ionic-like covalent bond: > 1.7

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how to identify if a molecule is polar or nonpolar

  1. polar bonds (electronegativity difference)

    • at least polar bond!!!

  2. shape/symmetry

    • asymmetrical = polar

    • symmetrical = non polar bc dipoles cancel e/o

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functional groups: hydroxyl (3)

what is the molecular formula? properties? (2) found in? (4)

  • molecular formula: (-OH)

  • properties: polar & electronegative

  • found in: Carbohydrates, proteins, nucleic acids, lipids

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functional groups: carbonyl (3)

what is the molecular formula? properties? (1) found in? (3) types? (2)

  • molecular formula: (-CO)

  • properties: polar

  • found in: Carbohydrates, nucleic acids, lipids

  • 2 types: aldehyde & ketone (refer to chemistry notes)

    • aldehyde: CO at one of the terminal carbon-end

    • ketone: CO at one of the internal carbons (O is double bonded to C, between 2 C)

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functional groups: carboxyl (3)

what is the molecular formula? properties? (3) found in? (2)

  • molecular formula: (-COOH)

  • properties: charged, ionizes to release H+, considered acidic bc release H+ into solution

  • found in: proteins, lipids

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functional groups: amino

what is the molecular formula? properties? (3) found in? (2)

  • molecular formula: (-NH3)

  • properties: charged, accepts H+, considered basic bc can remove H+ from solution

  • found in: proteins, lipids

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functional groups: phosphate

what is the molecular formula? properties? (2) found in? (1)

  • molecular formula: (-OPO32- or OPO3H2)

  • properties: polar, considered acidic

  • found in: nucleic acids

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functional groups: sulfhydryl

what is the molecular formula? properties? (3) found in? (1)

  • molecular formula: (-SH)

  • properties: polar, reducing agent, contribute to 3D structure of proteins

  • found in: proteins

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what are condensation reactions? be able to draw them.

  • = the removal of a hydrogen atom from the functional group of one subunit and an OH group from the other subunit’s functional group

  • creates a covalent bond b/w 2 subunits, linking them tgt

  • the OH and H come tgt to form a H2O molecule

  • results in formation of large molecules from smaller subunits

  • reverse of hydrolysis

  • = anabolic

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what are hydrolysis reactions? be able to draw them.

  • = the adding of an H atom to one subunit and an OH group to the other which were provided by a H2O molecule

  • H2O molecule is used to break a covalent bond holding subunits tgt

  • results in deformation of large molecules into smaller subunits

  • reverse of condensation reactions

  • = catabolic

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carbohydrates —

monosaccharides (1) composed of? vs

disaccharides (2) composed of? solubility? vs

polysaccharides (2) composed of? solubility?

  1. monosaccharides

  • single sugar molecule composed of C6, H12, O6

  1. disaccharides

  • composed of 2 monosaccharides joined tgt in a condensation reaction

  • hydrophilic and easily dissolve in water

  1. polysaccharides

  • a chain of monosaccharides

  • very polar → very hydrophilic, but bc very big → attract water & cannot dissolve

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lipids —

saturated (3) what bonds & state at room temp? structure? 2 examples? vs

unsaturated (3) what bonds & state at room temp? structure? 2 examples?

monounsaturated vs polyunsaturated

  1. saturated

  • single bonds

  • hydrocarbon chains are long & straight & packed closely tgt to form solid at room temp

  • e.g. butter, animals

  1. unsaturated

  • presence of double bonds creates a kink in molecule → causes bending

  • fluid & liquid at room temp bc not that closely packed tgt

  • e.g. olive oil/plants

  1. monounsaturated = fatty acid w/ one double bond

  2. polyunsaturated = fatty acid w/ 2 or more double bonds

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lipids —

triglyceride (3) composed of, what linkage, used for? vs

phospholipids (3) composed of? solubility? forms what when added to water?

triglyceride

  • composed of 3 fatty acids & glycerol

  • linkage bond is called ester linkage

  • used for long-term sugar storage or for insulation of a multicellular organism

phospholipids

  • glycerol attached to one phosphate group & 1 unsat. chain and 1 sat. chain

  • hydrophobic

  • form a sphere when added to water

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lipids — steroids (3) lack of? composed of? examples? (3) vs waxes (3) composed of? 3 properties? used for? (2)

steroids

  • NO fatty acids

  • made of 4 hydrocarbon rings w/ several diff functionals groups

  • e.g. cholesterol (found in plasma cell membrane in animal cells) & phytosterols (found in plant cells’ membranes) & makes hormones (i.e. estrogen, testosterone, progesterone)

waxes

  • composed of long fatty acid chains linked to OH or carbon rings

  • hydrophobic, non polar, soft solids

  • used as a barrier to infections & diseases, helps plants conserve water

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what is an isomer regarding to carbohydrates?

  • isomers have the same molecular formula but different arrangement of atoms

  • thus affecting biological functions

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carbohydrates — function (3)

  • primary source of energy (immediate & long-term)

  • provide structural support

  • cell to cell communication

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lipids — function (3)

  • energy storage

  • building membranes & other cell parts

  • insulation

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proteins — function (7)

  • alter rates of metabolic reactions

  • transport materials in cells or body

  • structural

  • blood clotting

  • part skin, tendons, ligaments

  • assist in metabolism

  • assist with immunity

25
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protein structure

primary vs secondary vs tertiary vs quaternary.

why/how does this happen?

  1. primary: sequence of amino acids in a linear sequence

  2. secondary: alpha-helix (helical shape) or beta-pleated sheet (folded shape)

  3. tertiary: additional folding & refining of chain as different “R” groups interact w/ e/o

  4. quaternary: 2 or more diff polypeptide chains combine to form a functional protein

why/how: specific sequence of amino acids strongly influences the protein’s biological function

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protein denaturing

what is it? why does it matter? (2)

  • protein denaturing = process where a protein unfolds & loses its specific structure

  • importance: it loses its biological function due to loss of specific 3D shape.

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fluid model of the cell membrane — structure

  • a mosaic of phospholipids, proteins, and carbohydrates

  • asymmetrical — half of the lipid bilayer differ from other half (diff functions)

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fluid model of the cell membrane — fluidity

  • fluidity is influenced by sterols (lipids)

  • e.g. cholesterol acts as membrane stabilizer — can decrease or increase fluidity by loosening or tightening space between phospholipids.

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fluid mosaic model of cell membrane & carbohydrates (2)

__ and _ faces the exterior of the cell? functions? (2)

  • glycolipids & glycoproteins face the exterior of the cell

  • function: identify “self” from “non-self” cells (crucial for immune system) & act as receptors for signalling hormones & neurotransmitters, relaying messages into the cell

30
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fluid mosaic model of cell membrane & lipids (2)

what lipid forms a ?

  • phospholipid form a bilayer - hydrophilic heads face outside & inside of the cell

  • hydrophobic fatty tails gather tgt inside

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fluid mosaic model of cell membrane & proteins:

integral proteins (2) what proteins are exposed to ? environment? made of ? regions to allow ?

& peripheral membrane proteins (3) where are they found?

  1. integral proteins

    • transmembrane proteins w/ regions exposed to the aqueous environment on both sides of the membrane

    • made of polar and non polar regions to allow their integration

  2. peripheral membrane proteins

    • on surface & DNI w/ hydrophobic core

    • mostly on cytosol (inside) side of the membrane & part of the cytoskeletal

    • structural

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passive transport (3) vs active transport (3)

passive

  • no energy required

  • movement from high conc. area to low conc. area

  • spreads out randomly

active

  • requires energy (ATP)

  • molecules move against the concentration gradient

  • carrier proteins are used to transport substances (e.g. ions)

    • (requires energy as it changes shape)

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passive transport — diffusion

what type of molecules can pass through?

__ conc to _ conc

examples?

  • free flowing

  • small non polar particles through concentration gradient

  • high conc. to low conc.

  • e.g. O2, CO2, (& H2O)

34
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passive transport — osmosis

movement of what?

from __ to _ solute conc?

moves from area of ? or ?? to an area w/ ?

  • movement of WATER

  • from low to high solute concentration

  • moves from area of PURE or more conc. SOLUTE (salts) to an area w/ more SOLVENTS (water)

35
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passive transport — osmosis

ISOTONIC VS HYPOTONIC VS HYPERTONIC

  1. isotonic = conc of both the solute & solvent is equal

  2. hypotonic = lower conc of solute & more solution

  3. hypertonic = higher conc & lower solution

36
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passive transport — facilitated diffusion

uses what to move through conc. gradient?

examples?

  • use of integral channel carrier proteins to move through concentration gradient

  • e.g. glucose, amino acids, sodium, H2O

  • water moves faster through aquaporin protein channels (Is this even on test)

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active transport — endocytosis

for bringing INTO or OUT of the cell?

what happens?

can be used for ? or for the cell to ?

  • bulk transport of large external or many small molecules INTO the cell

  • cell membrane engulfs particles w/ membrane and wraps them to form a vesicle

    • e.g. nutrients & signalling molecules

  • could be for cell use or for the cell to destroy

    • e.g. microphage

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active transport — exocytosis

what is it? uses? (2)

  • fusing vehicles with the cell membrane to release contents OUT of the cell

  • used for:

    • removing toxins or waste products from the cell’s interior

    • to move substances made in the cell to outside the cell to be used by the body

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