biological molecules Flashcards

(78 cards)

1
Q

why is water a polar molecule?

A
  • the oxygen atom pulls the shared electrons towards it
  • water is slightly negatively charged at the oxygen and positively charged at the hydrogen ends
  • they can form hydrogen bonds with each other.
  • This are continuing breaking and reforming, so the molecules can move around.
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2
Q

structure of am amino acid

A
  • amine group H2N
  • carboxyl group COOH
  • carbon in the centre-C
  • single hydrogen groupH
  • r group varies with different amino acid R-
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3
Q

primary structure

A

The sequence of amino acids found in a protein molecule

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4
Q

secondary structure

A

The coiling or folding of parts of an amino acid chain

due to hydrogen bond formation between different parts of the chain.

The main forms of secondary structure are the alpha helix and the beta pleated sheet

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5
Q

tertiary structure

A

The overall three-dimensional structure of a protein molecule.

It is the result of interactions between parts of the protein molecule such as hydrogen bonding, formation of disulfide bridges and hydrophobic interactions

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6
Q

quaternary structure

A

Protein structure where a protein consists of more than one polypeptide chain.

Haemoglobin has a
quaternary structure as it is made up on four polypeptide chains.

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7
Q

properties of water

A
  • solvent
  • provides an effective transport medium
  • form a major component of the tissues in living organisms
  • coolant
  • provide habitats for living things in rivers, lakes and seas
  • allows ionic compounds to separate
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8
Q

fibrous protein

A
  • has a relatively long, thin structure
  • is insoluble in water
  • metabolically inactive
  • structural role within an organism
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9
Q

globular protein

A
  • has molecules of a relatively spherical shape
  • soluble in water
  • often have metabolic roles within the organism
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10
Q

prosthetic group/haem

A

a non-protein component that forms a permanent part of a functioning protein molecule

the non protein component of a conjugated protein

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11
Q

amino acids

A

monomers of all proteins

all amino acids have the same basic shape

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12
Q

peptide bond

A

a bond formed when two amino acids are joined by a condensation reaction

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13
Q

lipids

A

a group of substances that are soluble in alcohol rather than water

include triglycerides, phospholipids, glycolipids and cholesterol

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14
Q

macromolecule

A

a very large, organic molecule

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15
Q

phospholipid

A

molecule consisting of glycerol, two fatty acids and one phosphate group

insoluble in water

contains ester bonds

important in membrane structure

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16
Q

carbohydrates

A

a group of molecules containing C, H and O

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17
Q

condensation reaction

A

reaction that occurs when two molecules are joined together with the removal of water

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18
Q

hydrogen bond

A

a weak interaction that can occur when wherever molecules contain a slightly negatively charged atom bonded to a slightly positively charged hydrogen

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19
Q

hydrolysis reaction

A

reaction that occurs when a molecule is split into two smaller molecules with the addition of water

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20
Q

monomer

A

a small molecule which binds to many other identical molecules to form a polymer

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21
Q

polymer

A

a large molecule made from many smaller molecules called monomers

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22
Q

alpha- glucose

A

glucose in which the hydrogen atom on carbon atom number one projects above the plane of the ring

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23
Q

ab initio protein modelling

A

a model built based on the physical and electrical properties of the atoms in each amino acid in the sequence

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24
Q

adhesion

A

the attraction between water molecules and the walls of the xylem vessel

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25
amylopectin molecule
a molecule of polysaccharide with glycosidic bonds between carbon 1 and 4, and branches formed by glycosidic bonds between carbon 1 and 6 it is a constituent of starch
26
amylose molecule
a molecule of polysaccharide with long straight chains of between 100 and 1000 alpha- glucose molecules it is a constituent of starch like maltose, it has glycosidic bonds between carbon 1 and 6
27
anion
a negatively charged ion
28
beta- glucose
glucose in which the hydrogen atom on carbon number one projects the plane of the ring
29
cation
a positively charged ion
30
chromatography
a technique for the separation of a mixture by passing it in solution or suspension through a medium in which the components of the mixture move at different rates
31
cohesion
the attraction between water molecules caused by hydrogen bonds
32
colorimeter
an instrument for measuring the absorbance of different wavelengths of light in a solution
33
comparative protein modelling
one approach is protein threading, which scans the amino acid sequence against a database of solved structures and produces a set of possible models which would match that sequence
34
computer modelling
a model of a process which is created on a computer, often used for processes that can need the increased calculation speed
35
conjugated protein
a protein associated with a non- protein component
36
conformational change
a change in the shape of a macromolecule
37
covalent bonds
formed when electrons are shared between atoms these bonds are very strong
38
deoxyribose
a five-carbon sugar derived from the five- carbon sugar ribose by replacement of a hydroxyl group by hydrogen, at carbon atom 2
39
disaccharides
any of a class of sugars whose molecules contain two monosaccharides residues joined by a condensation reaction
40
disulfide links/bridges/bonds
strong covalent bond (where electrons are shared) between two sulfur atoms, within a (protein) molecule. these bonds are bot broken by heat but can only be broken by reducing agents
41
elastin
a type of protein made by cross- linking a polypeptide called a tropoelastib- which has a coiled structure the cross-linking and coiling make elastin a strong and extensible protein. it is found in structures in living organisms, such as elastic cartilage and ligaments, where they need to stretch or adapt their shape as part of life processes
42
ester bond
a bond formed by condensation reaction between the OH group of a carboxylic acid and the OH group of an alcohol, to produce an ester
43
fatty acids
have a carboxyl group (COOH) on one end, attached to a hydrocarbon tail, made of only carbon and hydrogen atoms. this may be anything from 2 to 20 carbons long
44
glucose
a 6- carbon monosaccharide sugar
45
glycerol
has three carbon atoms. it is an alcohol, which means it has free- OH groups
46
glycogen molecule
the energy store in humans; large polysaccharide molecule made of many glucose residues joined by condensation reactions like amylopectin, has glycosidic bonds between carbon atoms 1 and 6
47
glycolipid
lipid/phospholipid with a chain of carbohydrate molecules attached
48
glycoprotein
protein with a chain of carbohydrate molecules attached
49
glycosidic bond
a bond formed between two monosaccharides by a hydrolysis reaction
50
haemoglobin
the red pigment used to transport oxygen in the blood hydrophobic groups on the inside polypeptide chains
51
hydrogencarbonate ion
HCO3-
52
hydrophilic
attracted to water
53
hydrophobic
repelled by water
54
inorganic ions
charged particles of inorganic (not carbon-based) substances (e.g Mg2+, Ca2+)
55
keratin
a fibrous protein forming the main structural constituent of hair, feathers, hooves, nails, claws, horns
56
lipids
a group of substances that are soluble in alcohol rather than water. they include triglycerides, phospholipids, glycolipids and cholesterol
57
lipophilic
attracted to fat (lipids)
58
lipophobic
repelled by fat (lipids)
59
macromolecule
a very large, organic molecule
60
pepsin
an enzyme that digests protein in the stomach of mammals
61
peptide bond
a bond formed when two amino acids are joined by a condensation reaction
62
polar
where the charge is not evenly distributed across a particle
63
polypepide
polymer made of many amino acids units joined together by peptide bonds. insulin is a polypeptide of 51 amino acids
64
polysaccharides
polymers of monosaccharides that re made of hundreds or thousands of monosaccharide monomers bonded together
65
proteins
large polymers comprised of long chains of amino acids
66
qualitative testing
test that shows the presence or absence of a substance but does not indicate how much of the substance is present
67
triglycerides
lipid molecules consisting of glycerol, and three fatty acids contains only C, H and O insoluble in water contains ester bonds
68
unsaturated fatty acid
fatty acid lacking the full complement of hydrogens. there are double bonds between some of the adjacent carbon atom, giving a kink in the long hydrocarbon chain
69
globular proteins
spherical hydrophilic on outside, hydrophobic on inside form hydrogen bonds with water soluble haemoglobin, pepsin, insulin
70
fibrous proteins
linear chain chains can form hydrogen bonds with adjacent chains within a molecule insoluble/ few hydrophilic groups strong have a structural role
71
haemoglobin
transports oxygen contains prosthetic group to allow oxygen to be carried tertiary structure
72
collagen
high proportion of glycine so chains lie close together forms covalent bonds between molecules cross links are staggered to avoid weak points forms part of tendons/ ligaments/ cartilage/ bone
73
cholesterol
only contains C,H and O insoluble in water important in membrane structure
74
amylose structure
coiled alpha-glucose, 1-4 glycosidic bonds all monomers in same orientation granular hydrogen bonds within molecule
75
cellulose structure
beta glucose, 1-4 glycosidic bonds alternative monomers at 180* to each other fibrous hydrogen bonds between adjacent molecules
76
cellulose properties
strong hydrogen bonds form insoluble forms cell walls
77
collagen structure
peptide bonds between amino acids every 3rd amino acid is the same/glycine coil 3 polypeptide chains, hydrogen bonds between fibril crosslinks
78
emulsion test for lipids
add ethanol stir add to water