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72 Cards in this Set
- Front
- Back
Vitalism |
Theory that the phenomena of life is due to a vital principle. (requires living things to be made). |
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Example of Vitalism |
Urea production in a living organism (thought only able to be produced by the kidney) Ammonia (NH3) + carbon dioxide (CO2) = Ammonium Carbonate (NH4CH2O2N) = Urea (CH2ON2) + Water (H2O) |
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types of bonds carbon can form |
Single Bond - one pair of shared electrons. Double Bond - two pairs of shared elections. Triple Bond - three pairs of shared electrons. |
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Define macromolecules and examples. |
Four main classes of Carbon Compounds - carbohydrates - lipids - proteins - nucleic acids |
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Glucose |
Six membered rings with one side chain |
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What does metabolism consist of |
Anabolism and Catabolism |
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Anabolism |
synthesis of complex molecules from simpler molecules including the formation of macromolecules by condensation reactions. e.g. protein and DNA synthesis |
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Catabolism |
breakdown of complex molecules into simpler molecules including hydrolysis of macromolecules into monomers. e.g. digestion of food |
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What are the four things a carbon atom will bond with. |
Amine Group (NH2) Carboxyl Group (COOH) A hydrogen atom (H) the R group (Protein) |
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Properties of water |
cohesion thermal adhesion solvent |
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Cohesion |
Hydrogen bonding causes water molecules to stay close to each other. |
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Adhesion |
this property occurs as a result of the polarity of a water molecule and its ability to form hydrogen bonds |
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High specific heat capacity |
The amount of heat needed for 1g of a substance to change its temperature by 1 degree. |
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High heat of vaporization |
the quantity of heat a liquid must absorb for 1g to be covered to the gaseous state. |
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solvent |
dissolving agent |
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solute |
the substance that is dissolved |
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solution |
a liquid that is a homogenous mixture of two or more substances |
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aqueous solution |
water is the solvent |
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Hydrophilic |
Water loving. All substances that dissolve in water are hydrophilic, including polar molecules |
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Carbohydrates |
a monosaccharide, disaccharide or polysaccharide. |
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Monosaccharide |
a single sugar unit. e.g. glucose, fructose, ribose |
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disaccharide |
consists of two monosaccharides joined by a covalent bond. linked by condensation reaction (creation of water). glucose + glucose = maltose + water. |
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polysaccharides |
consist of many monosaccharide units linked together. e.g. starch, glycogen, cellulose all are composed of glucose molecules linked in different ways. |
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starch |
made by plant cell and used to store large amounts of glucose. energy store (glucose molecules can be added or removed). |
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two forms of starch |
amylose (unbranched) amylopectin (branched). |
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Cellulose |
Unbranched chains of beta-glucose. hydrogen bonds link the molecules together. linked molecules form bundles called cellulose microfibrils |
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What is different about cellulose compared to other carbohydrates? |
very high tensile strength. we can’t break it down. |
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Glycogen |
similar to amylopectin, but more branching. made by animals and some fungi stored in the liver and some muscles in humans functions to store energy in the form of glucose |
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Fatty acids |
chain of carbon atoms linked by a covalent bond contain a carboxyl group at one end. |
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Three types of fatty acids |
can be saturated, monounsaturated or polyunsaturated |
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Saturated |
if there are only single bonds between the carbon atoms, then each carbon atom is bonded to as many hydrogen atoms as possible. |
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Unsaturated |
if there are one or more double bonds between the carbon atoms. |
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monounsaturated |
one double bond |
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polyunsaturated |
more than one double bond |
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isomer |
molecules with the same number and type of atom, but with a different arrangement of those atoms |
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trans isomer |
hydrogens are on the opposite end of the double bond |
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difference between isomer and trans isomer |
trans isomers are rare in nature and usually artificially produced to produce solid fats e.g. margarine from vegetable oils |
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cis isomer |
hydrogens are on the same side of the double bond. opposite of trans isomers |
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Triglycerides |
formed by condensation from three fatty acids and one glycerol. |
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what makes lipids more advantageous to animals than carbohydrates? |
suitable for long term energy storage in humans than carbohydrates. a gram of fat stores more than twice as much energy as a gram of polysaccharide (starch). animals must carry their energy stores with them, so it is advantageous to have a more compact reservoir of food. |
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Where is fat stored in animals. |
fat is stored in adipose cells, which form adipose tissue. adipose tissues cushion vital organs like kidneys. adipose tissue beneath the skin also serves as a layer of insulation |
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Equation for Body Mass Index (kgm^2) (BMI) |
mass (kg) / (height (m)^2 |
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Nomogram |
alternative to calculating BMI ruler is used to draw a line from the body mass to height.Where the drawn line intersects the W/H2 line is the BMI. |
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Ribosomes |
the molecules within cells that facilitate the formation of peptide bonds. |
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Polypeptide |
linked amino acids forming proteins, coded by an R group. |
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Genes |
unit of inheritance consisting of a specific DNA sequence. |
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How many amino acids are there in a polypeptide? |
4 to thousands |
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Central Dogma of Genetics |
DNA -> RNA -> Polypeptide or basically Gene -> Message -> Product |
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Four levels of protein structure |
Primary Secondary Tertiary Quaternary |
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Primary Protein Structure |
- Amino acid sequence - peptide bonds - the order/number of amino acids in a polypeptide chain - the primary structure is read from the NH2— terminal to the —COOH terminal. - each amino acid is identifies by its specific R group - most polypeptides are between 50-1000 amino acids long |
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Secondary Protein Structure |
- repeating local structures - held by H-bonds - local folding of the polypeptide backbone - stabilized by H-bonds - three types of secondary structures: - alpha (helix) - beta (pleated sheet) - open loops |
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Tertiary Protein Structure |
- folding of a single protein - R-group interactions - hydrophobic core - 3D conformation of a polypeptide - amino acid chain (in the helical, pleated or loop form) links itself in places to form the unique twisted or folded shape of the protein. - stabilized by R-group interactions - hydrophobic core - 3D structure gives proteins their functional properties such as active sites on enzymes. |
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Quaternary Protein Structure |
- Protein complex - Made of two or more subunitsnumber of tertiary polypeptides are joined together. - composed of four different polypeptide chains - each chain forms a tertiary structure called a haem group. - e.g. haemoglobin |
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Prosthetic Groups |
proteins are often bound to inorganic groupse.g. Haemoglobin has four polypeptide “haem” groups each associated with and FE2+ |
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What are the two types of proteins and their functions? |
Fibrous - structural roles Globular - functional |
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Denaturation |
process in which the protein unravels and loses its native state. |
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What happens during denaturation? |
- Protein becomes inactive - interactions between R-groups are interrupted - heat causes denaturation by breaking interactions between r-groups - pH affects charges in R-groups, which disrupts interactions. |
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Functions carried out by proteins |
Catalysis -> Tensile Strengthening Muscle Contraction -> Blood Clotting Cytoskeleton -> Transport of nutrients and gases Cell Adhesion -> Receptors Membrane Transport -> Hormones Immunity -> Packing of DNA e.g. rubisco, insulin, immunoglobins, rhodopsin, collagen and spider silk |
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Proteome |
all the proteins produced by a cell, a tissue, or an organism a proteome is variable as different cells will make different proteins |
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Genomes |
what proteins an organism can make |
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Enzymes |
globular proteins used as catalysts for biochemical reactions speeds up reactions without being consumed |
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Substrate |
Reactant in a biochemical reaction |
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Active Site |
region on the surface of an enzyme to which substrates bind and which catalyses the reaction |
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Collision |
the coming together of an active site and substrate |
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How do active sites and substrates match each other? |
structurally, the 3d structure of the active site is specific to the substrate. substrates that don’t fit won’t react chemically, substrates that are not chemically attracted to the active site won’t be able to react. |
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Effects of Temperature on Collisions |
- as temperature increases, rate of reaction increases - as molecules have more energy, move faster and collide and react more frequently - optimum temperature = maximum rate of reaction - balance between enzyme stability and kinetic energy of reactants - at too high of a temperature however, enzyme is denatured |
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Substrate Concentration |
- increase in concentration of substrate molecules results in increase in rate of reaction. - levelled makes optimal - too high, makes full saturation, rate becomes constant, any increase beyond the optimum will have no added effect because no extra active site to be used. |
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Denaturation |
- loss of r group interactions - change in structure means change in active site - if it changes shape, no longer able to bind to substrates |
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Lactose |
The natural sugar found in milk. Some people are lactose intolerant using enzymes, lactose free milk can be made |
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Commercial Uses |
- many enzymes have commercial uses - e.g. detergents - proteases and lipases, breakdown protein and fat stains. - biofuels - breakdown starch in grains - brewing - clarification - medicine and bioengineering - diagnostics, contact lens cleaner. - always immobilized enzymes - attached to a material so movement is restricted |
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Common ways to immobilize enzymes |
- aggregations of enzymes bonded together - attached to surfaces like glass - entrapped in gels, like alginate gel beads. |
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Advantages of immobilizing enzymes |
- enzymes are easily separated from the product - retrieved enzymes can be used again - increases stability of enzymes - substrates can be exposed to higher enzyme concentration |