Biomolecules

• The 5 main elements in Biomolecules: Carbon, Hydrogen, Oxygen, Nitrogen, Phosphorus, Sulfur. Carbon is usually the skeleton.
• POLYMERIZATION / CONDENSATION / DEHYDRATION SYNTHESIS

  • The creation of polymers by DEHYDRATING two monomers
• Adding H2O to BREAK bonds
• Carbohydrates

  • Uses:
  • Building materials
  • Provide energy and fuel (From the sugars they contain)
  • For Complex sugars: Oligosaccharides and polysaccharides, provides structural support and energy storage
  • Combines with amines, lipids, and amino acids to perform functions
  • Have sugars and polymers
  • (CH2O)n general formula
• MONOSACCHARIDES (Monomers)

  • Simple sugars. The building blocks of Carbohydrates
  • Combine to make polymers (Disaccharides, Oligosaccharides, Polysaccharides)
  • Has -OH (Hydroxyl group) attached to each C EXCEPT 1. C is double bonded to O (Carbonyl group)
  • Aldoses (Aldehyde Sugars)
  • Attached to end of Carbon skeleton
  • Ketoses (Ketone sugars)
  • Attached in the middle of the Carbon skeleton
  • Trioses (3 carbon sugars), Pentoses (5 carbon sugars), Hexoses (6 carbon sugars)
  • EXAMPLES:
  • Glucose (Synthesis of fatty acids and amino acids)
  • C1 bonds to C5
  • Galactose
  • Fructose
• DISACCHARIDES

  • Two sugars
  • Linked together by a Glycosidic linkage
  • C12H22O11
  • Examples: 
  • Glucose + Glucose -> Maltose
  • Glucose + fructose -> Sucrose
  • Glucose + Galactose -> lactose
• OLIGOSACCHARIDES

  • Polymers linked together by Glycosidic bonds
  • Homopolysaccharide - polymers are the same
  • Heteropolysaccharide - polymers are different
• POLYSACCHARIDES

  • Starch (Storage)
  • Made up of glucose monomers
  • For energy storage in plants
  • Amylose - Unbranched
  • Amylopectin - Branched
  • Glycogen (Storage)
  • Extensively branched
  • Energy storage in animals
  • Cellulose
  • Major component of cell wall in plants and algae
  • Unbranched polymer of glucose
  • Chitin
  • Monomer is an amino sugar
• Lipids

  • Unique as they are not polymers
  • Hydrophobic since mostly made up of C-H bonds
• FATS/OILS

  • Usages:
  • Insulation
  • Cushion vital organs
  • Energy storage (Excess glucose is transformed into this)
  • Triacylglycerol / triglycerides
  • Glycerol (Backbone) + 3 Fatty acids
  • Found in adipose cells
  • Is a rich source of energy (more than carbohydrates)
  • Ester linkage - Reaction between hydroxyl and carbonyl group to form fats
• • Saturated Fatty Acids
  • Single bonds between C
  • Maximum number of Hydrogen atoms + straight shape, which makes it very stable and solid
  • Unsaturated Fatty Acids
  • Have two or more bonds between C
  • Kinking of the shape, unstable at room temperature (exists as oil)
  • Hydrogenated fats
  • Unsaturated fatty acids converted into saturated fats
  • Trans fats
  • Partially hydrogenated unsaturated fatty acids
• PHOSPHOLIPIDS

  • Major constituent of cells
  • Components: Glycerol backbone, 2 fatty acids, 1 phosphate containing group, 1 small charged polar molecule
• STEROIDS

  • Backbone of four interlocking carbon rings
  • Cholesterol
  • Component of cell membranes
  • Vitamin D synthesis
  • Precursors of estrogen and testosterone
  • Synthesized in the liver and obtained from diet
  • Bile Acids
  • Vitamins
  • Steroid hormones
• Proteins

  • Polymers of amino acids (polypeptides)
  • Linked together by a peptide bond 
  • Same covalent bond from dehydration synthesis
  • Most important, abundant, diverse
  • C, H, O and N
  • Structural components of membranes, cells, tissues
  • Hormones and enzymes
• AMINO ACIDS

  • Building blocks of proteins. 20 naturally occurring amino acids.
  • Contain
  • Amino group (base)
  • Carboxyl group (acid)
  • Variable group R
  • Will dictate the properties of the amino acid
  • Hydrogen at the bottom of the alpha carbon
  • Amino acid and carboxyl group on either side of the C.
  • Non-polar (Hydrophobic)
  • Polar (Hydrophilic)
  • Electrically charged (Hydrophilic)
  • 9 Essential Amino Acids
  • Can only be from proteins in the died (Cannot be synthesized by the body)
• POLYPEPTIDE

  • Polypeptide has backbone
  • Amino end (N-terminus)
  • Carboxyl end (C-terminus, COOH)
  • Side chains with different r groups
• A polypeptide can be considered as a protein if and only if it serves a biological function. A protein may have one or more polypeptides.
• Protein structure depends on the function and the dictated shape of proteins

  • Conformation (Shaping) will determine specific function
• PROTEIN FOLDING

  • Protein spontaneously folds for proper biological function
  • While cell synthesizes proteins, it folds
  • Misfolding may cause loss of structure and folding
• PRIMARY STRUCTURE

  • Tells how many, what kinds, and the order of amino acids
  • DNA tells what amino acids for cells to make
  • Transthyretin
  • Globular - roughly spherical
  • 4 polypeptides
• SECONDARY STRUCTURE

  • Folding of polypeptide chain 
  • Results form the formation of hydrogen bonds between atoms in the backbone
  • Helix (Coiled)
  • Pleated sheet
• TERTIARY STRUCTURE

  • Gives final 3D shape of the polypeptide
  • Side chains are involved instead of the backbone
  • I Have Had Dinner
  • Ionic bond 
  • Hydrophobic bond
  • Hydrogen bond
  • Disulfide bond
• QUATERNARY STRUCTURE

  • Applicable to only two or more polypeptides
  • Not applicable to single polypeptide
  • Chains are stabilized by intermolecular interactions
  • Hemoglobin
• • Denaturation Change in confirmation which leads to loss of biological function and activity
  •  (Up to the 2nd level)
  • Renaturation - restore native state when returned to normal environment
  • Not all denaturation can be reversed (When primary level is affected)
• Enzymes

  • Organic catalyst
  • Speeds up the biochemical reaction
  • Not changed by the reaction or consumed
  • Works only for a VERY specific function. Very choosy with its environment. Effective in small amounts and is reusable. It is synthesized by the cell.
  • Lowers energy of activation for the chemical reaction
  • Substrate - the reactant an enzyme acts on (Must have complementary shapes)
  • Enzyme-substrate complex
  • Active site - Where the enzyme inserts itself into the substrate.

  Mostly made up of proteins (Made of Amino acids with R group)
• SUCRASE

  • Hydrolysis of sucrose catalyzed by sucrase
  • Cofactors - Mineral ions required for activation
  • Coenzymes - act as a carrier of small chemical groups that are removed from the substrate
• Nucleic Acids

  • Blueprints of Life
  • Gives instruction on how to make protein molecules (needed to develop, grow, survive, and reproduce)
  • Nucleotides - building blocks of nucleic acids -> polynucleotides
  • Joined by phosphodiester bonds
  • Storage, replication, recombination, transmission
  • Two types: DNA (deoxyribonucleic acid / sugars part of the nucleotide) RNA (Ribonucleic acid)

  Components: Phosphate group (PO4), Pentose sugar, nitrogenous base (this is the one that differs. Holds genetic info and are hydrophobic)
• • Purines: 
  • Has 2 fused rings: a 5 and a 6 membered ring
  • Bigger than pyrimidines
  • Adenine (Has 2 partners)
  • Guanine (Has 1 partner)
  • Cannot partner with pyrimidines because the diameter of the DNA won't be retained
• • Pyrimidines: 
  • Has only 1 6 membered ring
  • Thymine (Partners w/ adenine)
  • Cytosine (Partners w/ guanine)
  • Uracil (Partners w/ adenine)
• NUCLEIC ACIDS

  • Phosphate + sugar group of another molecule to link backbone
  • 5’ to 3’ direction
  • TA  / UA, GC
  • DNA double helix 
  • Compact
  • Protect genetic information
  • Nitrogenous base is hydrophobic so it goes inside