biology - biological molecules

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100 Terms

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covalent bonding
atoms share a pair of electrons in their outer shells
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ionic bonding
ions with opposite charges attract each other - electrostatic attraction
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hydrogen bonding
electrons within a molecule not evenly distributed - one region more negatively charged = polar
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what do polymers usually contain?
carbon, hydrogen, oxygen and nitrogen
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condensation reaction
joins two molecules together with the formation of a chemical bond and involves the elimination of a molecule of water
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hydrolysis reaction
breaks a chemical bond between two molecules and involves the use of a molecule of water
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what is metabolism?
all the chemical processes that take place in living organisms
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why is carbon often used in polymers?
carbon atoms can bond with each other to form a carbon sequence - a backbone
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what is a monomer?
the smaller units from which larger molecules are made
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examples of monomers
monosaccharides, amino acids and nucleotides
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2 isomers of glucose
alpha and beta glucose
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what is a reducing sugar?
a sugar that can donate electrons to another chemical
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what is the test for reducing sugars?
add 2 cm3 of the food sample to a test tube

add 2cm3 Benedict’s reagent to test tube

heat for 5 minutes in water bath
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what is the positive result when testing for reducing sugars?
colour change:

green and yellow = low concentration

orange = medium

brick-red = high
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glucose + glucose
maltose
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glucose + galactose
lactose
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glucose + fructose
sucrose
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what is the bond formed when monosaccharides bond?
glycosidic bond
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what is an example of a non-reducing sugar?
sucrose
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what is the test for non-reducing sugars?
add 2cm3 of food sample and 2cm3 hydrochloric acid to a test tube

heat for 5 minutes - HCl will hydrolyse any disaccharide present

slowly add sodium hydrogencarbonate solution to test tube - neutralise HCl

heat with 2cm3 Benedict’s reagent for 5 minutes
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what is the positive result when testing for a non-reducing sugar?
Benedict’s reagent will turn orange-brown
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what is a property of all polysaccharides?
insoluble - suitable for storage
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where is starch found?
plants - in the form of small grains
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what is the test for starch?
place sample into a spotting tile

add 2 drops of iodine
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what is the positive result when testing for starch?
colour changes from orange to blue-black
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what is starch made up of?
amylose and amylopectin
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structure of amylose
1,4 glycosidic bonds

unbranched chain

coiled, very compact
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structure of amylopectin
1,4 and 1,6 glycosidic bonds

branched - hydrolysed quickly to release energy
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properties of starch
insoluble - doesn’t affect water potential of cell

large, compact

branched - hydrolysed quickly to form alpha glucose which can be used in respiration
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what type of glucose is glycogen and starch made up of?
alpha glucose
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what bonds are in glycogen?
1,4 and 1,6 glycosidic bonds
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properties of glycogen
main storage molecule of animal cells

highly branched = rapidly hydrolysed

compact

insoluble - doesn’t affect water potential of cells
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what type of glucose is cellulose made up of?
beta glucose
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structure of cellulose
straight, unbranched chains - run parallel to each other, allowing hydrogen bonds to form cross-linkages between adjacent chains

cellulose molecules group together to form microfibrils - arrange in parallel groups called fibres
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what is the purpose of cellulose?
major component of plant cell walls - provides rigidity, prevents cell bursting due to osmotic pressure caused by entry of water, makes cell turgid
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2 types of lipids
triglycerides and phospholipids
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roles of lipids
phospholipids in cell surface membrane - contribute to flexibility and transfer of lipid-soluble substances

source of energy

waterproofing

insulation

protection
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structure of triglycerides
three fatty acid chains and glycerol head - each fatty acid forms an ester bond with glycerol during condensation reaction
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what does an unsaturated triglyceride have?
at least one carbon carbon double bond
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how does the structure of triglycerides relate to their properties?
high ratio of energy-storing carbon-hydrogen bonds = good energy source

low mass to energy ratio = good storage molecules

insoluble in water = doesn’t affect water potential of cells
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structure of phospholipids
hydrophilic phosphate head, glycerol backbone, 2 hydrophobic fatty acid tails
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how does the structure of phospholipids relate to their function?
polar = in an aqueous environment they form a bilayer within cell-surface membranes

phosphate heads help to hold at the surface of the cell-surface membrane

structure allows them to form glycolipids by combining with carbohydrates in the cell-surface membrane = important in cell recognition
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what are the similarities between the two types of lipids?
contain carbon, hydrogen and oxygen

insoluble in water

soluble in organic solvents

all contain ester bonds
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what are the differences between the two types of lipids?
t = 3 fatty acid chains, p = 2 fatty acid chains

p = hydrophilic phosphate head
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what is the test for lipids?
add 2cm3 of sample and 5cm3 ethanol to test tube

shake tube to dissolve any lipid

add 5cm3 water and shake
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what is the positive result when testing for lipids?
milky-white emulsion
47
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how many amino acids occur in all living organisms?
20
48
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what is the structure of an amino acid?
what is the structure of an amino acid?
amino group: N-H-H

carboxyl group: COOH

hydrogen atom: H

R group
amino group: N-H-H

carboxyl group: COOH

hydrogen atom: H

R group
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what is the bond between amino acids in polypeptides?
peptide bond (between carbon of one AA and nitrogen of other AA)
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what is the primary structure of proteins?
polypeptide chain - peptide bonds between amino acids
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what is the secondary structure of proteins?
alpha helix or beta pleated sheet

contains hydrogen bonds
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what is the tertiary structure of proteins?
further folded, 3D

bonds = disulfide bridges, ionic bonds, hydrophobic-hydrophilic
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what is the quaternary structure of proteins?
more than 1 polypeptide chain

may also contain a prosthetic group (non-protein)
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give an example of a protein that has a tertiary structure
enzymes
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give an example of a protein that has a quaternary structure
haemoglobin - 4 polypeptide chains and 4 haem (iron) groups
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what is the test for proteins?
place sample in test tube and add Biuret solution (sodium hydroxide solution + copper II solution)
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what is the positive result when testing for proteins?
colour change from blue to violet
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what type of proteins are enzymes?
globular
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what are enzymes?
biological catalysts
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what is the purpose of enzymes?
lower activation energy of reactions
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where on the enzyme does the substrate bond?
active site
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what is formed when a substrate binds to an active site?
enzyme-substrate complex
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explain the induced fit model of enzyme action
the active site changes shape to fit the substrate
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explain the lock and key theory
the substrate fits the active site perfectly - complementary shapes
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what factors affect enzyme action?
temperature, pH, enzyme concentration, substrate concentration
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how do we measure the progress of an enzyme-catalysed reaction?
formation of the products of the reaction and the disappearance of the substrate
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explain the effect of temperature on enzyme action
* a rise in temperature increases the kinetic energy of molecules - the molecules move around more rapidly and collide with each other more often = more enzyme-substrate complexes
* temperature rise also causes the bonds in the enzyme molecule to break - active site changes shape, substrate no longer fits = less or no enzyme-substrate complexes formed
* enzyme finally denatures - no longer works
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explain the effect of pH on enzyme action
a change in pH alters the charges on the amino acids that make up the active site of the enzyme - the active site changes shape and the substrate no longer fits, enzyme-substrate complex can’t be formed
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explain the effect of enzyme concentration on the rate of reaction
* once an active site on an enzyme has acted on a substrate, it is free to repeat the procedure on another substrate molecule = enzymes work efficiently at low concentrations
* as long as there is an excess of substrate, an increase in the amount of enzyme leads to a proportionate increase in the rate of reaction
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explain the effect of substrate concentration on the rate of enzyme action-
* if the concentration of enzyme is fixed and substrate concentration is slowly increased, the rate of reaction increases in proportion to the concentration of substrate
* when there is an excess of substrate the rate of reaction plateaus
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competitive inhibitors
* they have a molecular shape similar to the substrate = they occupy the active site - block it
* the difference between the concentration of the inhibitor and the concentration of the substrate determines the effect on enzyme activity
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non-competitive inhibitors
* attach themselves to the enzyme at the binding site (not the active site) - the inhibitor alters the shape of the active site so the substrate can no longer bind
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what does DNA stand for?
deoxyribonucleic acid
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what are nucleotides made up of?
* pentose sugar
* phosphate
* a nitrogen-containing base
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what are the 5 bases called?
pyrimidine bases = cytosine, thymine and uracil

purine bases = adenine and guanine
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what is the bond called that is formed between two nucleotides?
phosphodiester bond
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what is the structure of RNA (ribonucleic acid)?
* single polynucleotide chain
* pentose sugar a ribose sugar
* bases = adenine, guanine, cytosine and uracil
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who discovered the structure of DNA?
Watson and Crick
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what is the structure of DNA?
* pentose sugar - deoxyribose
* bases - adenine, thymine, guanine, cytosine
* made up of 2 polynucleotide strands - double helix
* strands joined together by hydrogen bonds
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what are the base pairings?
adenine with thymine - 2 hydrogen bonds

cytosine with guanine - 3 hydrogen bonds
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what is the function of DNA?
the hereditary material responsible for passing information from cell to cell and generation to generation
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how is DNA adapted to carry out its functions?
* a very stable structure which normally passes from generation to generation without significant change
* 2 strands are joined only with hydrogen bonds - allow them to separate during DNA replication and protein synthesis
* large = carries an immense amount of genetic information
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what is DNA replication called and why?
semi-conservative replication - double helix made up of one new strand and one old strand
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describe the process of semi-conservative replication
* DNA helicase breaks the hydrogen bonds linking the base pairs of DNA
* double helix unwinds
* each exposed polynucleotide strand acts as a template - free complementary nucleotides bind by specific base pairing
* DNA polymerase joins nucleotides
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describe the structure of ATP
* adenine
* ribose sugar
* 3 phosphates
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how does ATP store energy?
the bonds between phosphate groups are unstable so have a low activation energy = easily broken, release a considerable amount of energy
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what is the equation for the hydrolysis of ATP?
ATP + H2O --→ ADP+ Pi
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what enzyme is used during the synthesis of ATP?
ATP synthase
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what is the role of ATP?
immediate energy source - hydrolysis of ATP to ADP a single reaction
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which processes is ATP used in?
* metabolic processes - build up polymers
* muscle contraction
* active transport
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what type of molecule is water?
polar - oxygen atom slightly negative, hydrogen atom slightly positive, the positive pole of one water molecule attracted to the negative pole of another water molecule
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what are the properties of water?
* high specific heat capacity
* high latent heat of vaporisation
* cohesion - water molecules stick together (e.g. in xylem)
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what is the importance of water to living organisms?
* water the main constituent of all organisms
* water used in hydrolysis reactions
* chemical reactions take place in an aqueous medium
* water used in photosynthesis
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how is water used as a solvent?
water dissolves other substances: gases, wastes, inorganic ions, enzymes
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what are other important features of water?
* evaporation cools organisms and allows them to control their temperature
* not easily compressed so provides support
* transparent - aquatic plants can photosynthesise
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where are inorganic ions found?
in organisms where they occur in solution in the cytoplasm of cells and in body fluids, as well as part of larger molecules
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iron ions
found in haemoglobin where they play a role in the transport of oxygen
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phosphate ions
form a structural role in DNA molecules and a role in storing energy in ATP molecules
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hydrogen ions
important in determining the pH of solutions and therefore the functioning of enzymes
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sodium ions
important in the transport of glucose and amino acids across plasma membranes