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Biological molecules

Structure and properties of different biological molecules

TermDefinition
Maltose a-glucose + a-glucose - reducing
Lactose a-glucose + b-galactose - reducing
Sucrose a - glucose + fructose - non reducing
What are the properties and structure of Cellulose? Long, straight, unbranched polymer of 1,4 linked b-glucose with every 2nd molecule flipped to form strands. H bonds hold chains together forming parallel Microfibrils-> Macrofibrils. Uses: Durable, insoluble, strong, stabilized and slightly elastic-->Pre
Starch - structure? Helix (Covalent and H bonds) Amylose - Compact spiral stabilized by H bonds Unbranched chains of 1000's of 1,4 linked a-glucose Amylopectin - shorter branched chains of 1.4 a-glucose and 1,6 links (branch 'ends' for enzymes)
Glycogen Larger branched polymer of a-glucose(1,4 and 1,6 linkages), easily hydrolyzed due to lots of 'ends'. Uses: Energy reserve for respiration in Liver, Muscle fibers and bodily tissues except brain
Monosaccharides Glucose, fructose, galactose, Deoxyribose(C6), ribose(C5), glyceraldehyde
Triglycerides Structure: 3 Fatty acids (sat or unsat) + 1 Glycerol (3 ester bonds) Non-polar, hydrophobic molecule
Phospholipids Hydrophilic(polar) phosphate head + 1 Glycerol + Hydrophobic(non-polar) 2 fatty acid tails (2 ester bonds)
Describe the formation of Triglycerides Condensation reaction ->> Water + COO ester linkage between glycerol (OH) and 3 fatty acids (COOH)
Describe formation and functions of Phospholipids Condensation reaction->> Water and 2 ester bonds Phospholipid Bilayer membrane - hydrophilic heads facing outwards and tails facing inwards
Properties of Triglycerides Energy storage - more C-H compared to Carbs, more energy per unit mass. Metabolic water source, Buoyancy aid, Waterproofing (marine animals), Electrical insulation -myelin sheath, Low mass, Large and insoluble - don't affect water potentials and osmosis
Protein structure and examples Amine grp + C- H and R grp + COOH e.g. collagen, haemoglobin, enzymes, antibodies, keratin, Transporter proteins
List the bonds in a polypeptide in order of increasing strength Hydrophobic (non-polar R grps) interactions Hydrogen, Ionic (ionized amine and carboxylic acid grps) Covalent (disulfide and peptide)
Peptide bond Strong covalent bond(C-N), formed from Condensation between 2 amino acids
Formation of polypeptide Synthesized at Ribosome; Condensation reaction; Very strong, covalent Peptide linkages CONH = COOH + Nh2. Polypeptide -> Hydrolysis ->amino acids (Reverse condensation)
Cysteine and Glyceine Cysteine R = Sulphur HS - CH2 - CHNH2 - COOH Glyceine R grp= H --> H2N - CH2 - COOH
Primary Unfolded, specifically sequenced amino acid chain - peptide bonds only
Secondary Folded polypeptide with either A -helix (H2 bonds between -NH and -CO) B-pleated sheet - straight looser, parallel flat sheets
Tertiary Precise 3D folded polypeptide due to side chain interactions All 4 bonds e.g. Myoglobin with haem grp
Quaternary E.g. Collagen and Haemoglobin - 2 a-chains and 2 b-chains 2 or more polypeptides All 4 bonds includes all levels of structure
Globular protein Spherical, ball shape, Soluble (Most tertiary, some quaternary). e.g. All enzymes, antibodies, myoglobin, haemoglobin, some hormones
Fibrous protein Long & Parallel strands, Insoluble (Most 2ndary + forms fibers) - Collagen, Keratin
Collagen 3 polypeptide triple helix held by H bonds form a fibre. Parallel, staggered ends - High tensile strength
Haemoglobin Properties - Highly soluble due to hydrophilic R grps facing outwards and hydrophobic R grps facing inwards Bind to oxygen - change shape to increase oxygen affinity + 4 haem Fe2+ ions to bind to 4 O2 molecules.
Water properties and why? Excellent solvent- dipolar surrounds polar mols(transport of substances and metabolic reactions) High specific heat cap - stable environment temp High latent heat of vaporisation and fusion - cooling effect and protection from cold
Created by: user-1992837
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