all

• LIPIDS = storing energy, signaling between cells, and forming the cell membrane
• LIPIDS = made up of fatty acids
• LIPIDS = INSOLUBLE IN WATER ; HYDROPHOBIC ; NON POLAR
• SATURATED FATS = STRIAGHT CARBON CHAINS
• SATURATED FAT = SOLID AT ROOM TEMP

  • butter
• UNSATURATED FAT= HAS DOUBLE / TRIPLE BOND
• UNSATURATED FAT = LIQUID AT ROOM TEMP

  • olive oil
• TRIGLYCERIDES = STORES ENERGY

  • 1 glycerol - 3 fatty acid
• HYDROLYZABLE LIPID

  • WAX
  • GLYCOLIPIDS
  • PHOSPHOLIPIDS
• NON-HYDROLYZABLE

  • STEROIDS
  • FAT SOLUBLE VITAMINS
• FAT SOLUBLE VITAMINS = VITAMIN : A ; D ; E ; K
• BROMINE TEST FOR LIPIDS = UNSATURATION

  • [ + ] CLEAR SOL
  • [ - ] BROWN PPT
• PROTEIN = GREEK WORD: PROTEIOS

  • MEANING : primary
• PROTEINS = CONTAINS AMINO GROUP & CARBOXYL GROUP
• AMINO ACIDS = BODY: L-isomers & alpha-carbon
• R group in protein gives each amino acids = IDENTITY
• AMIDE BOND = PEPTIDE BOND
• PEPTIDE BONDS = FORMED BY CONDENSATION reaction
• BIURET TEST

  • In the presence of an alkaline solution, Cu2+ ion forms as a complex with the peptide bonds due to the unshared electron pairs in nitrogen, and the oxygen in the water. 
• NINHYDRIN = CAUSES oxidative decarboxylation and deamination of α-amino acids

  • PRODUCT : ALDEHYDE ; CO2 ; AMMONIA
• XANTHOPROTEIC TEST

  • aromatic nucleus + conc nitric acid HNO3 = YELLOW SOL
  • aromatic nucleus + conc nitric acid HNO3 + excess NaOH = ORANGE-RED SOL
• MILLON TEST

  • Tyrosine is first nitrated by nitric acid in the test solution, then the nitrated tyrosine complexes mercury (I) and mercury (II) = RED PPT / SOL
• HOPKIN-COLE TEST

  • The indole reacts with glyoxylic acid in the presence of a strong acid = VIOLET CYCLIC
• LEAD SULFIDE

  • The organic sulfur in cysteine or cystine is released as inorganic S-8 ions which form lead sulfide = BLACK / BROWN PPT
• PROTEINS = CONTAINS: CARBON ; HYDROGEN ; OXYGEN ; NITROGEN ; SULFUR
• PROTEIN = HIGHLY SPECIFIC
• PROPERTIES OF PROTEINS

  • COLORLESS & TASTELESS
  • HOMOGENOUS & CRYSTALLINE
  • GLOBULAR & FIBROUS
  • AMPHOTERIC ; ACID / BASE
• ALBUMIN

  • HEAT COAGULABLE
  • WATER SOLUBLE
  • PRESENT : EGG WHITE ; MILK ; SERUM
• GLYCOCONJUGATE PROTEIN : EGG WHITE ; MILK

  SIMPLE PROTEIN : SERUM
• CASEIN = CHIEF PROTEIN OF MILK

  • PHOSPHOPROTEIN
  • NON HEAT COAGULABLE
  • INSOLULE IN WATER
  • SOLUBLE IN DILUTED ACIDS / ALKALI
  • CONTAINS CYSTEINE / CYSTINE
• GELATIN = LOW BIOLOGICAL VALUE PROTEIN

  • INSOLUBLE IN COLD WATER
  • SOLUBLE IN HOT WATER
  • NON HEAT COAGULABLE
  • DERIVED FROM COLLAGEN
  • DOES NOT CONTAIN : TRYPTOPHAN
• DENATURATION =  loss of the secondary, tertiary, and quaternary structures of a protein by a chemical or physical agent that leaves the primary structure intact. 
• DENATURATION = The disruption of the primary protein structure occurs with the hydrolysis of the peptide bonds to produce free amino acids. 
• FACTORS INFLUENCING PROTEIN DENATURATION

  • Strong acids and bases
  • Organic Solvents
  • Reducing Agents
  • Salt Concentration
  • Heavy Metals
  • Temperature Change
  • Mechanical Stress
• ENZYME = a macromolecule that catalyzes a biochemical reaction
• SUBSTRATES = STARTING MOLECULES
• Enzymes work by LOWERING THE ACTIVATION ENERGY needed to make a chemical reaction occur
• KEY FEATURE OF ENZYME = SPECIFIC
• ENZYMES = GLOBULAR PROTEIN
• Substrates initially bind to the active site by noncovalent interactions, including hydrogen bonds, ionic bonds, and hydrophobic interactions.