Lesson 4 - Proteins Flashcards

1
Q
A
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2
Q

what are amino acids

A

the building blocks of proteins, consisting of an amino group and a carboxyl group attached to a carbon atom and an R group that varies between amino acids

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3
Q

what are peptide bonds

A

a bonds formed by condensation reactions between amino acids

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4
Q

what are dipeptide bonds x

A

2 amino acids joined by a peptide bond

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5
Q

what are polypeptides

A

long chains of amino acids joined by peptide bonds

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6
Q

what are fibrous proteins

A

proteins that have long, parallel polypeptide chains with occasional cross-linkages that form into fibres, but with little tertiary structure

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7
Q

what are disulfide bonds

A

a strong covalent bond formed as a result of an oxidation reaction between sulfur groups in cysteine or methionine molecules, which are close together in the structure of a polypeptide

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8
Q

what are globular proteins

A

large proteins with complex tertiary and sometimes quaternary structures, folded into spherical shapes

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9
Q

what is haemoglobin

A

a large conjugated protein involved in transporting oxygen in the blood, and gives the erythrocytes their red colour

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10
Q

what is collagen

A

strong fibrous protein with a triple helix structure

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11
Q

what is denaturing

A

the loss of the 3D shape of a protein as a result of changes in pH or temperature

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12
Q

what is the prosthetic group

A

a molecule that is added in a conjugated protein

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13
Q

what is a glycoprotein

A

a protein with a carbohydrate prosthetic group

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14
Q

what is protease

A

a protein-digesting enzyme

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15
Q

what is a lipoprotein

A

a protein with a lipid prosthetic group

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16
Q

which elements are proteins made up of

A

carbon, hydrogen, oxygen, nitrogen (& sulfure)

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17
Q

how many different types of amino acids are there

A

20

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18
Q

what is the R group

A

another atom or group of atoms bonded to the central atom

19
Q

how is a protein formed

A

amino acids join together by a condensation reaction where 1 molecule of water is lost. A strong peptide bond is formed between the 2 amino acids, forming a dipeptide. The R group is not involved. More amino acids join to form a polypeptide. When the polypeptide folds or coils, it forms a protein

20
Q

what are the 4 types of bonds between amino acids

A
  • peptide bonds
  • hydrogen bonds
  • disulfide bonds
  • ionic bonds
21
Q

how is a hydrogen bond formed

A

in amino acids, when negative charges on the oxygen of the carboxyl groups and positive charged on the hydrogen atoms of the hydroxyl group come close together, the opposite charges attract, forming a weak hydrogen bond.

22
Q

how is a disulfide bond formed

A

when 2 cysteine molecules are close together in a polypeptide. An oxidation reaction takes place between the 2 sulfur-containing groups, resulting in a strong disulfide bond

23
Q

what is the nature of hydrogen bonds

A

break easily, but are very common

24
Q

what is the nature of disulfide bonds

A

stronger than hydrogen bonds, and occur less often

25
how is an ionic bond formed
form between strongly positive and negative amino acid side chains in protein molecules.
26
what is the nature of ionic bonds
strong, but rarely occur
27
which protein is hair made out of
keratin
28
how does blow drying or straightening affect the protein keratin
it breaks the hydrogen bonds and reforms them temporarily in a different way, until the hydrogen bonds reform in their original places
29
how does perming affect the protein keratin
it breaks the disulfide bonds between the polypeptide chains, and permanently reforms them, until cut
30
what is the primary structure
the linear sequence of amino acids in a peptide
31
what is the secondary structure
folding or coiling of the polypeptide chain, such as an alpha-helix or beta-pleated sheets
32
what is the tertiary structure
the 3D folding of the secondary structure
33
what is the quaternary structure
the 3D arrangement of more than one tertiary polypeptide
34
what is the function of collagen
gives strength to tendons, ligaments, bones and skin, as it is very strong
35
what is the structure of collagen
It's made up of 3 polypeptide chains. The primary structure of the chains is repeating sequences of glycine with proline and hydroxyproline. The 3 alpha-chains are arranged in a triple helix, held together by many hydrogen bonds
36
what are collagen fibres
collagen molecules held together with fibrils
37
what is the genetic disease osteogenesis imperfecta
where the collagen triple helix may not form properly. As a result, the bone lacks tensile strength, becoming brittle and breaking easily
38
what is the role of globular proteins
important in the immune system (antibodies), form enzymes and hormones, and maintain the structure of the cytoplasm
39
explain how the structure of hemoglobin makes its job
it is the iron that enables the haemoglobin to bind and release oxygen molecules
40
what is the function of glycoprteins
the carbohydrate prosthetic group helps them hold on to a lot of water, and makes it harder for proteases to break them down
41
what is the function of lipoproteins
important in the transport of cholesterol the blood, as it enables it to combine with the lipid cholesterol
42
what are the 2 types of lipoproteins
Low-Density Lipoproteins (LDLs) High-Density Lipoproteins (HDLs)
43
what is the difference between LDLs and HDLs
HDLs contain more proteins and are smaller than LDLs,