2.2 BIOLOGICAL MOLECULES Flashcards

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1
Q

What is biochemistry?

A

Biochemistry is chemical reactions involving biological molecules

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2
Q

What are most abundant bio moles?

A

The most abundant bio moles are carbon, oxygen, nitrogen, sulfur and phosphorus.

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3
Q

What are monomers?

A

Monomers are single, small molecules capable of joining together to form a polymer

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4
Q

What are polymers?

A

Polymers are large molecules made up of many identical monomers

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5
Q

What is are condensation and hydrolysis reactions?

A

Condensation reactions covalently bond monomers together to form polymers are release monomers. Hydrolysis reactions add water to break those bonds

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6
Q

What is an ion?

A

An ion is an atom or group of atoms that carry a positive (cations) or negative (anions) charge.

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7
Q

What are cations necessary for?

A

Cations are necessary for:
Ca2+ = nerve impulse transmission muscle contraction
Na+ = nerve impulse transmission kidney function
K+ = nerve impulse transmission stomata openings
H+ = catalysis of reactions pH determination
NH4+ = production of nitrate ions by bacteria

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8
Q

What are anions necessary for?

A

Anions are necessary for:
NO3- = nitrogen supply to plants
HCO3- = maintenance of blood pH
Cl- = balance positive charge of Na and K ions
PO4- = cell membrane, nucleic acid and ATP formation
OH- = catalysis of reactions pH determination

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9
Q

Why does water contain hydrogen bonds?

A

Water contains hydrogen bonds as water is polar. Oxygen is slightly more delta negative than hydrogen and so the negative charge is pulled closer to oxygens nucleus

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10
Q

What are the properties of water?

A

The properties of water are:
- cohesive (attraction of other molecules of the same kind)
- adhesive (attraction of other molecules of a different kind, xylem function)
- high specific heat capacity (preventing temperature fluctuations, absorb large amounts of heat)
- high latent heat of vaporisation (water removes heat as it evaporates, moderates earths climate and prevents organisms overheating)
- density (ice less dense than liquid = floats)
- solvent (dissolves other substances)
- transparency (light can pass through)

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11
Q

What are monosaccharides?

A

Monosaccharides are any of the class of sugars that cannot be hydrolysed to give a simple sugar.
- general formula (CH2O)n
- same number C and O atoms
- white crystalline solides
- dissolve in water to form sweet tasting solutions

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12
Q

What are isomers?

A

Isomers are molecules that have the same chemical formula but different structural formulae

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13
Q

What are the properties of glucose?

A

The properties of glucose are:
- polar and soluble in water
- number of polar OH groups attached to carbons
- hydrogen bonds can form between OH groups (causes glucose to dissolve)
- soluble in cytosol of cells

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14
Q

What are discaccharides?

A

Disaccharides are molecules formed from two monosaccharides joined together by a glycosidic bond
- general formula C12H22O11
-crystalline water

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15
Q

What is a polysaccharide?

A

Polysaccharides are large molecules made of many smaller monosaccharides joined together by glycosidic bonds
- general formula Cx(H20)y
- can be linear or branched
- function in organisms is often storage or structure related
- often insoluble molecules

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16
Q

Why are polysaccharides formed?

A

Polysaccharides are formed as glucose must be stored appropriately in cells as it is soluble- meaning it would effect the osmotic properties of the cells, so it is stored as polysaccharides which are insoluble. Glucose needs to be stored as when it breaks down in respiration it releases ATP. Animals only have the enzymes to break down alpha glucose, not beta glucose

17
Q

Amylose and amylopectin structure and function.

A

Amylose is an alpha-glucose molecule, in the shape of an alpha helix with 1-4 glycosidic bonds. It is found in plant cells and is used as an energy store in plants.
Amylopectin is also an alpha-glucose molecule, but is highly branched and contains 1-4 and 1-6 glycosidic bonds

18
Q

Cellulose structure and function.

A

Cellulose is a beta-glucose molecule with 1-4 glycosidic bonds in a long chain. It contains fibres/fibrils and is found in plant cells. Cellulose forms the plant cell wall

19
Q

Glycogen structure and function.

A

Glycogen is a alpha-glucose molecule with 1-4 and 1-6 glycosidic bonds. It is highly branched and found in animal cells. It is used as an energy store.

20
Q

What are the uses of lipids?

A

The uses of lipids are:
- energy storage
- membrane component
- insulation (thermal and mechanical)
- waterproofing
- hormones
- source of energy

21
Q

What are lipids?

A

Lipids are a group of macromolecules that are not polymers. They include triglycerides and are non-polar. They include phospholipids and steroids, e.g cholesterol waxes

22
Q

What are triglycerides?

A

Triglycerides are made from 3 fatty acids and a glycerol, joined together by ester bonds. They are a triester of glycerol.
They are formed by a condensation reaction between the carboxyl group of the fatty acid and hydroxyl group of glycerol

23
Q

Saturated and unsaturated fatty acids.

A

Saturated fatty acids do not contain a double bond, unsaturated do.

24
Q

What are phospholipids?

A

Phospholipids are similar to triglycerides but are 2 fatty acids bonded to the glycerol, with a phosphate group covalently bonded to the 3rd.
- have a hydrophobic region (head)
- have a hyrophillic region (tail)

25
Q

What is cholesterol?

A

Cholesterol are complex alcohol molecules with a hydroxyl group at one end (OH).
- have hydrophobic and hydrophillic ends
- can fit between phospholipids and help regulate fluidity in membranes
- stops membrane being flimsy and gives membrane rigidity

26
Q

Facts about proteins.

A

Proteins are:
- CHONS
- broken down by protease
- made from long chained amino acids (polymers)
- form over 50% cells dry mass
- consist of one or more polypeptides arranged as complex macromolecules and have specific biological functions

27
Q

What is the amino acid structure?

A

Amino acid structure:
hydrogen
amine - C - carboxyl
R-group

28
Q

Peptide-dipeptide formation.

A

Peptide-dipeptide formation:
- condensation and hydrolysis happens in the same way as in polysaccharide formation (peptide bond formed in process)
- all peptides will have an amino acid end and carboxyl end

29
Q

What are polypeptides?

A

Polypeptides are:
- lots of amino acids joined together
- polymers and macromolecules
- formation of peptide bonds takes place at ribosomes and is catalysed by enzyme peptidyltransferase

30
Q

Protein structure.

A

Levels of protein structure:
1. primary - sequence of amino acids
2. secondary - O, H and N atoms of amino acids interact and form hydrogen bonds and leads to formation of alpha helix (chain of amino acids coiled due to hydrogen bonding with attractions forming between O in -CO on an amino acid or H in -NH on an amino acid 4 places ahead) or beta pleated sheets (polypeptide chains that lie parallel to one another joined by hydrogen bonds)
3. tertiary structure - coils and pleats start to fold, held together by; hydrogen bonds, hydrophobic and hydrophillic between polar and non-polar R-groups, disulphide bridge
- denatured by heating
4. quaternary - interaction of two or more individual proteins (polypeptide chains) called subunits

31
Q

Protein bonding.

A

Protein bonding:
- hydrophobic parts of the R-groups move to the centre of the polypeptide to avoid water, whereas hydrophillic parts move towards the water
- causes the twisting of amino acid chain which changes shape to form globular proteins
- makes protein water soluble as water molecules can easily cluster around them

32
Q

Fibrous proteins.

A

Fibrous proteins:
- long, insoluble molecules
- high proportion of amino acids with hydrophobic R-groups
- primary structure is repetitive
e.g collagen- consists of 3 polypeptide chains crosslinked by numerous hydrogen bonds and wrapped in triple helix
- hydrogen bonds form staggered ends between adjacent collagen molecules (allow for attachment of proteins and each end- forming tropocollagen)
- many collagen molecules form a fibril which link to form fibres
- contains high proportions of amino acids
- found in skin, tendons, ligaments and other tissues
e.g keratin- rich in cysteine so lots of disulfide bridges making keratin strong, inflexible and insoluble
- provides mechanical protection
- waterproof
- found in fingernails, hair, horns, scales, fur, feathers
e.g elastin- cross-linking and coiling make structure strong and flexible
- found in lungs, bladder, skin, lining blood vessels

33
Q

Globular proteins.

A

Globular proteins:
- almost spherical in shape
- soluble in water groups
- compact
e.g insulin- made of two polypeptide chains
- hormone un regulating blood glucose levels
- needs to be soluble to be transported in the blood
e.g conjugated proteins- contain non-protein element (prosthetic group)
e.g haemoglobin- quaternary structure
- made up of 2 alpha-globin and 2 beta-globin polypeptide chains
- a haem group in each subunit (molecule of O can bind to each haem group)
e.g catalase- quaternary protein with 4 haem prosthetic groups
- allows catalase to interact with hydrogen peroxide to speed up its breakdown