knowt logo

Biology: Unit 1 Review

  • Carbon: backbone of all biological molecules, makes ring, chains & branches

  • Polar: Hydrophilic

  • Non-polar: Hydrophobic

  • Acids are a H+: donor

  • Bases are a H+: Accept-or

  • C:H:O → 1:2:1

  • Glycosidic : linkages between carbohydrates

  • Monosachardies: Energy & Building. Made of ring/chain & hydroxyl. Glucose, ribose, deoxyribose.

  • Disacharide: Energy. Made of 2 units w/ an alpha or beta linkage. Hydroxyl. Sucrose, maltose, lactose.

  • Polysacharide: Storage, structure & communication. Chains and branches. Hydroxly. Starch & cellulose.

  • Glu + Gal = Lactose

  • Glu + Glu = Maltose

  • Glu + Fru = Sucrose

  • Fatty acids: Energy and cellular function. Hydrocarbon chain w/ carboxyl (+ hydroxyl) on the end. Non-polar.

  • Saturated fatty acid: single linked carbon bonds in a chain

  • Unsaturated fatty acids: 2+ carbon bonds in a chain (kinks)

  • Fat: Storage and insulation. Made of fatty acids chains and glycerol. carboxyl (+ hydroxyl). Butter & olive oil. Non-polar.

  • Triglycerides: 3 chains on the glycerol

  • Saturated fat: saturated chains that are straight and allow the substances to thicken

  • Unsaturated fat: kinky, unsaturated chains that dont let substance get thick and stay fluid

  • Esther linkage: linkage joining glycerol + fatty acid chains

  • Phospholipids: cell membrane bi-layer. Phosphate, glycerol, 2 chains & a polar unit. Non-polar. carboxyl (+ hydroxyl).

  • Steroids: hormones & cell response. 4 rings with 17 carbons. Hydroxly. Testosterone, cholesterol. Non-polar.

  • Wax: Water resistance. Long chains with alcohol rings in between. carboxyl (+ hydroxyl). Stuff on fruits, trees or stems. Non-polar.

  • Enzyme: biological catalyst with specific 3d shape.

  • Activite sites on enzyme are specific to: particular substrates.

  • Enzyme activity is affected by: substrate and enzyme concentrations, temp & pH.

  • Competitive inhibitors: enter binding site to block substrate.

  • Noncompetitive inhibitors: attach to another site to change enzyme shape and block substrate.

  • Allosteric regulation: inhbit (inhibitor) or stimulate (activator) enzyme activity by altering affinity of site for substrate.

  • Induced fit: not a perfect fit at first but changes shape to workout

  • Cofactor: non-protein sidekicks that activate enzyme by adjusting the fit for substrate

  • Reversible inhibition: weak binding, enzyme returns to normal after

  • Irreversible inhibition: strong binding, enzyme is fully disabled

  • Hydroxyl: Polar, soluble. Alcohols and carbs. Ethyl or glucose.

  • Carbonyl: Polar, soluble. Aldehydes and ketone. Acetone.

  • Carboxyl: Ionic, soluble, acidic (low pH). Carbonyl + Hydroxyl. Organic acids. Acetic acid (vinegar).

  • Amine: Ionic, soluble, basic (high pH). Amino acids. Alanie or cystine.

  • Phosphate: Ionic, soluble, acidic. Nucleic acids. G3P. Negatively charged when loosing H+.

  • Sulfhydryl: Non-polar, insoluble, di-sulfide bridges. Cystine or mercaptoethanol.

  • Primary structure: Amino acids → Peptide

  • Secondary structure: → Polypeptide

  • Tertiary structure: → Protein

  • Quaternary structure: → Functioning protein

  • Peptide bonds: N-C-C → N-C-C

  • Denaturation: happens when protein faces extreme pH, Temp, Salinity or Chemical change

  • Dehydration: process used to form glycosidic, esther, phosphodiesther & peptide linkages

  • Nucleotides → Nucleid acid (DNA/RNA) → Amino Acids

  • Nucleotides are made up of: Phosphate, 5C sugar & Bases.

  • Bases: adenine (A), cytosine (C), guanine (G), and thymine (T). Uracil (U) in RNA.

  • Purines: double ringed, A, D

  • Pyrimidines: single ringed, T/U, C

  • Dehydration synthesis: water is removed so 2 units can join

  • Hydration synthesis: water is added to so 2 units can break down

  • Buffer: maintains proper pH level when compensation is needed

  • Amylose: unbranched helical plant starch, energy storage

  • Amylopectin: branches helical plant starch, energy storage

  • Animal starch: glycogen, energy storage

  • Cellulose: plant cell wall, extensive hydrogen bonding, strong and tightly packed

  • Chitin: fungal cell wall, insect exoskeleton

  • How much the human body is water? 60%

  • The polarity of water leads to the formation of hydrogen bonds.

  • H2O is the reactant in a hydrolysis reaction.

  • Hydrogen bonding creates surface tension in water.

  • Proteins are used to convey genetic information.

  • Enzymes allow: digestion, light energy reactions in chloroplasts & cooler body temp for reactions

  • Water is LESS dense at cooler temperatures. Ice floats.

  • Enzymes are dependent on other molecules to function.

AV

Biology: Unit 1 Review

  • Carbon: backbone of all biological molecules, makes ring, chains & branches

  • Polar: Hydrophilic

  • Non-polar: Hydrophobic

  • Acids are a H+: donor

  • Bases are a H+: Accept-or

  • C:H:O → 1:2:1

  • Glycosidic : linkages between carbohydrates

  • Monosachardies: Energy & Building. Made of ring/chain & hydroxyl. Glucose, ribose, deoxyribose.

  • Disacharide: Energy. Made of 2 units w/ an alpha or beta linkage. Hydroxyl. Sucrose, maltose, lactose.

  • Polysacharide: Storage, structure & communication. Chains and branches. Hydroxly. Starch & cellulose.

  • Glu + Gal = Lactose

  • Glu + Glu = Maltose

  • Glu + Fru = Sucrose

  • Fatty acids: Energy and cellular function. Hydrocarbon chain w/ carboxyl (+ hydroxyl) on the end. Non-polar.

  • Saturated fatty acid: single linked carbon bonds in a chain

  • Unsaturated fatty acids: 2+ carbon bonds in a chain (kinks)

  • Fat: Storage and insulation. Made of fatty acids chains and glycerol. carboxyl (+ hydroxyl). Butter & olive oil. Non-polar.

  • Triglycerides: 3 chains on the glycerol

  • Saturated fat: saturated chains that are straight and allow the substances to thicken

  • Unsaturated fat: kinky, unsaturated chains that dont let substance get thick and stay fluid

  • Esther linkage: linkage joining glycerol + fatty acid chains

  • Phospholipids: cell membrane bi-layer. Phosphate, glycerol, 2 chains & a polar unit. Non-polar. carboxyl (+ hydroxyl).

  • Steroids: hormones & cell response. 4 rings with 17 carbons. Hydroxly. Testosterone, cholesterol. Non-polar.

  • Wax: Water resistance. Long chains with alcohol rings in between. carboxyl (+ hydroxyl). Stuff on fruits, trees or stems. Non-polar.

  • Enzyme: biological catalyst with specific 3d shape.

  • Activite sites on enzyme are specific to: particular substrates.

  • Enzyme activity is affected by: substrate and enzyme concentrations, temp & pH.

  • Competitive inhibitors: enter binding site to block substrate.

  • Noncompetitive inhibitors: attach to another site to change enzyme shape and block substrate.

  • Allosteric regulation: inhbit (inhibitor) or stimulate (activator) enzyme activity by altering affinity of site for substrate.

  • Induced fit: not a perfect fit at first but changes shape to workout

  • Cofactor: non-protein sidekicks that activate enzyme by adjusting the fit for substrate

  • Reversible inhibition: weak binding, enzyme returns to normal after

  • Irreversible inhibition: strong binding, enzyme is fully disabled

  • Hydroxyl: Polar, soluble. Alcohols and carbs. Ethyl or glucose.

  • Carbonyl: Polar, soluble. Aldehydes and ketone. Acetone.

  • Carboxyl: Ionic, soluble, acidic (low pH). Carbonyl + Hydroxyl. Organic acids. Acetic acid (vinegar).

  • Amine: Ionic, soluble, basic (high pH). Amino acids. Alanie or cystine.

  • Phosphate: Ionic, soluble, acidic. Nucleic acids. G3P. Negatively charged when loosing H+.

  • Sulfhydryl: Non-polar, insoluble, di-sulfide bridges. Cystine or mercaptoethanol.

  • Primary structure: Amino acids → Peptide

  • Secondary structure: → Polypeptide

  • Tertiary structure: → Protein

  • Quaternary structure: → Functioning protein

  • Peptide bonds: N-C-C → N-C-C

  • Denaturation: happens when protein faces extreme pH, Temp, Salinity or Chemical change

  • Dehydration: process used to form glycosidic, esther, phosphodiesther & peptide linkages

  • Nucleotides → Nucleid acid (DNA/RNA) → Amino Acids

  • Nucleotides are made up of: Phosphate, 5C sugar & Bases.

  • Bases: adenine (A), cytosine (C), guanine (G), and thymine (T). Uracil (U) in RNA.

  • Purines: double ringed, A, D

  • Pyrimidines: single ringed, T/U, C

  • Dehydration synthesis: water is removed so 2 units can join

  • Hydration synthesis: water is added to so 2 units can break down

  • Buffer: maintains proper pH level when compensation is needed

  • Amylose: unbranched helical plant starch, energy storage

  • Amylopectin: branches helical plant starch, energy storage

  • Animal starch: glycogen, energy storage

  • Cellulose: plant cell wall, extensive hydrogen bonding, strong and tightly packed

  • Chitin: fungal cell wall, insect exoskeleton

  • How much the human body is water? 60%

  • The polarity of water leads to the formation of hydrogen bonds.

  • H2O is the reactant in a hydrolysis reaction.

  • Hydrogen bonding creates surface tension in water.

  • Proteins are used to convey genetic information.

  • Enzymes allow: digestion, light energy reactions in chloroplasts & cooler body temp for reactions

  • Water is LESS dense at cooler temperatures. Ice floats.

  • Enzymes are dependent on other molecules to function.