CARBOHYDRATES, LIPIDS, AND PROTEINS Flashcards

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1
Q

monomers and polymers

A
  • Monomers are individual molecules that make up a polymer.
  • Polymers are long chains that are composed of many individual
    monomers that have been bonded together in a repeating pattern.
  • Condensation Reactions occurs when two
    molecules combine to form a more complex
    molecule with the removal of water.
  • Hydrolysis Reactions occurs when larger
    molecules are broken down into smaller
    molecules with the addition of water.
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2
Q

carbohydrates

A
  • Monosaccharides are the simplest carbohydrates, consisting of
    only one sugar molecule (e.g. Glucose, Fructose &
    Galactose).
  • Ribose sugars (pentose) are found in many important
    biological molecules such as ribonucleic acid (RNA),
    ATP, NAD
  • Glucose is a hexose sugar with 2 isomers
  • Disaccharides are sugars that are composed
    of two monosaccharides joined together in a
    condensation reaction, forming a glycosidic bond
    Maltose - 2 × α-glucose
    Sucrose - α-glucose and fructose
    Lactose - β-glucose and galactose
  • Polysaccharides are formed by many monosaccharides joined
    together.
    ◦ Amylose, amylopectin (starch) is the main polysaccharide
    energy store in plants, is composed of ž-glucose.
    ◦ In animals, the polysaccharide energy store is called
    glycogen, composed of ž-glucose.
    ◦ Cellulose is a structural component of plant cell walls
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3
Q

lipids

A

Fatty acids can be:
◦ Saturated – there are no C=C bonds and the molecule has as
many hydrogen atoms as possible.
◦ Unsaturated – there is at least one C=C bond, therefore the
molecule contains fewer hydrogen atoms than is maximally
possible.
* A triglyceride molecule is formed by joining one molecule
of glycerol to three fatty acids through three condensation
reactions, forming ester bonds.
* Triglycerides have key
roles in respiration and
energy storage due to
its insolubility and high
carbon to hydrogen ratio.
* Phospholipids replace one of the fatty acid chains in
triglycerides with a phosphate molecule.
* The hydrophobic tails
and hydrophilic heads of
phospholipids allow them to
form phospholipid bilayers.

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4
Q

proteins

A
  • Amino acids are the monomer units used to make proteins.
  • The 20 naturally occurring amino acids only diff er in their R groups.
  • Dipeptides are formed when two
    amino acids are joined together
    by a condensation reaction,
    forming a peptide bond.
  • A polypeptide is a polymer
    made of many amino acids
    joined together by peptide
    bonds.
  • A protein may contain one or more polypeptide chains
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5
Q

globular proteins

A
  • A globular protein is protein with a spherical shape that is
    soluble in water; they typically have metabolic roles
  • Globular proteins have a few important properties:
    ◦ They are roughly spherical in shape, with hydrophobic R
    groups on the inside and hydrophilic R groups on the outside.
    They are therefore soluble in water
    ◦ They have very specifi c shapes; this allows them to carry out
    very specifi c functions
  • Haemoglobin is a conjugated globular protein, made of 4
    polypeptide chains and 4 haem prosthetic groups which contain Fe2+.
  • Insulin is composed of two polypeptide chains, joined together
    by disulphide links. The specifi city of the shape allows binding
    to cell membrane receptors.
  • Pepsin has hydrogen bonds, disulphide link and few basic R
    groups to keep it functional in low pH stomach acid.
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6
Q

fibrous proteins

A
  • Fibrous proteins have some similar properties to each other:
    ◦ They contain long polypeptide chains with repeating
    sequences of amino acids
    ◦ The amino acids have non-polar R groups, so the proteins are
    insoluble in water
    ◦ The polypeptide chains are able to form fi bres which make
    the proteins stronger
  • Collagen is used to make bones, tendons and are found in
    artery walls to help resist the high pressure
  • Keratin contains high amounts of cysteine, resulting in disulphide
    links forming between the two polypeptide chains, which makes
    the molecule very hard and strong. It is found in fi ngernails,
    hooves and horns.
  • Elastin has the ability to stretch and recoil. Elastin is stretchy
    due to coiling of the elastin molecules and cross-links that keep
    the molecules together. It is found in the lungs, bladder and
    blood vessel walls.
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7
Q

inorganic ions

A
  • Inorganic ions are atoms or molecules with an electric charge,
    containing no carbon.
  • Cations are positively charged ions
  • Anions are negatively charged ions
  • Inorganic ions occur in solution in the cytoplasm and body
    fl uids of organisms, some in high concentrations and others in
    very low concentrations
  • Each type of ion has a specifi c role, depending on its properties
    ◦ Hydrogen ions determine the pH of bodily fl uids. The higher
    the concentration, the lower the pH
    ◦ Sodium ions are used in the co-transport of glucose and amino
    acids across cell membranes and transmission of nervous impulses
    ◦ Phosphate ions are essential components of DNA, RNA,
    nucleotides & ATP
    ◦ Calcium ions regulate protein channels, impulse transmission
    and harden body parts like teeth.
    ◦ Potassium ions play a role in muscle contraction, nervous transmission. active transport and maintaining turgidity in plant cells.
    ◦ Ammonium ions and Nitrate ions are part of the nitrogen
    cycle and a source of nitrogen for biological molecules
    ◦ Hydrogencarbonate ions are formed when carbon dioxide
    dissolves in blood. They are important in the transport of
    carbon dioxide in the blood and the regulation of blood pH
    CO2 + H2O ⇌ HCO3

    + H+
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8
Q
A
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9
Q

levels of protein structure

A
  1. Primary
    - The specific sequence of amino acids in a polypeptide chain
    - Peptide bonds
  2. Secondary
    - The curling or folding of the
    polypeptide chain into α-helices
    and β-pleated sheets due to the
    formation of hydrogen bonds
    - Hydrogen bonds
  3. Tertiary
    - The overall specific 3-D shape of
    a protein, which is determined by
    interactions between R groups
    and the properties of R groups
    - Hydrogen bonds
    - Ionic bonds
    - Disulphide bridges
  4. Quaternary
    - The specific 3-D shape of a
    protein that is determined by the
    multiple polypeptide chains and/or
    prosthetic groups bonded together
    - Hydrogen bonds
    - Ionic bonds
    - Disulphide bridges
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10
Q
A

1.Reducing sugars
- Benedict’s reagent → Heat Red/orange precipitate
- Reagent test strip
- Compare with calibration card

  1. Nonreducing sugars
    - Hydrochloric acid → Heat Sodium hydrogencarbonate
    - Benedict’s reagent → Heat
    - Red/orange precipitate
  2. Starch
    - Iodine in potassium iodide solution
    - Blue/black
  3. Proteins
    - Sodium hydroxide
    - Copper (II) sulphate
    - Purple
  4. Lipids
    - Ethanol
    - Water → Shake
    - Cloudy white
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