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AH Biology > 1.2c - Protein Structure, Ligand Binding and Conformational Change > Flashcards

1.2c - Protein Structure, Ligand Binding and Conformational Change Flashcards

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1
Q

Proteins are polymers of…

A

amino acid monomers

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2
Q

Amino acids are linked by peptide bonds to form…

A

polypeptides

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3
Q

The chemical structure of a peptide bond involves…

A

two amino acids (OH and H) joining together to form water

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4
Q

Amino acids have the same basic structure, differing only in…

A

the R group present

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5
Q

The R groups of amino acids vary in…

A

size, shape, charge, hydrogen bonding capacity and chemical reactivity

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6
Q

Amino acids are classified according to their R groups:

A

basic (positively charged), acidic (negatively charged), polar, hydrophobic

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7
Q

Basic amino acids have which R group?

A

NH2

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8
Q

Acidic amino acids have which R group?

A

COOH

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9
Q

Polar amino acids have which R group?

A

OH

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10
Q

Hydrophilic amino acids have which R group?

A

Hydrocarbon

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11
Q

The wide variety of functions carried out by proteins results from…

A

the diversity of R grouups

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12
Q

The primary structure is…

A

the sequence in which amino acids are synthesised into the polypeptide

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13
Q

Hydrogen bonding along the backbone of the protein strand results in…

A

regions of secondary structure

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14
Q

Regions of secondary structure include…

A

alpha helices, parallel or anti-parallel beta-pleated sheets, or turns

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15
Q

The polypeptide folds into…

A

a tertiary structure

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16
Q

The structure conformation is stabilised by…

A

interactions between R groups

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17
Q

Regions of tertiary structure include…

A

hydrophobic interactions, ionic bonds, London dispersion forces, hydrogen bonds, disulphide bridges

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18
Q

Disulphide bridges are…

A

covalent bonds between R groups containing sulphur

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19
Q

Quaternary structure exists in…

A

proteins with 2 or more connected polypeptide subunits

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20
Q

Quaternary structure describes…

A

the spatial arrangements of the subunits

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21
Q

A prosthetic group is…

A

a non-protein unit tightly bound to a protein and necessary for its function

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22
Q

The ability of haemoglobin to bind to oxygen is dependent upon the…

A

non-protein haem group

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23
Q

Interactions of the R groups can be influenced by…

A

temperature and pH

24
Q

Increasing temperature disrupts the interactions that…

A

hold the protein in shape causing it to unfold and eventually become denatured

25
Q

The charges on acidic and basic R groups are affected by…

A

pH

26
Q

As pH increases or decreases from the optimum, the normal ionic interactions between charged groups are…

A

lost, which gradually changed the conformation of the protein until it is denatured

27
Q

A ligand is…

A

a substance that can bind to a protein

28
Q

R groups not involved in protein folding can…

A

allow binding to ligands

29
Q

Binding sites will have complementary…

A

shape and chemistry to the ligand

30
Q

As the ligand binds to a protein-binding site…

A

the conformation of the protein changes

31
Q

The change in conformation of proteins causes a…

A

functional change in the protein

32
Q

Allosteric interactions occur between…

A

spatially distinct sites

33
Q

The binding of a substrate molecule to one active site of an allosteric enzyme increases…

A

the affinity of the other active sites for binding of subsequent substrate molecules

34
Q

The activity of allosteric enzymes can vary greatly with small changes in…

A

substrate concentration, which is of biological importance

35
Q

Many allosteric proteins consist of…

A

multiple subunits (have quaternary structure)

36
Q

Allosteric proteins with multiple subunits show co-operativity in binding, in which…

A

changes in binding at one subunit alter the affinity of the remaining subunits

37
Q

Allosteric enzymes contain…

A

a second type of site, called an allosteric site

38
Q

Modulators regulate the…

A

activity of the enzyme when they bind to the allosteric site

39
Q

Following the binding of a modulator…

A

the conformation of the enzyme changes and this alters the affinity of the active site for the substrate

40
Q

Positive modulators…

A

increase the enzyme’s affinity for the substance

41
Q

Negative modulators…

A

reduce the enzyme’s affinity for the substance

42
Q

Co-operativity is shown in haemoglobin by…

A

the binding and release of oxygen

43
Q

Changes in binding of oxygen alters…

A

the affinity of the remaining subunits for oxygen

44
Q

What influences and has physiological importance on the binding of oxygen?

A

temperature and pH

45
Q

A decrease in pH or an increase in temperature lowers…

A

the affinity of haemoglobin for oxygen, so the binding of oxygen is reduced

46
Q

Reduced pH and increased temperature in activity of respiring tissue will…

A

reduce the binding of oxygen to haemoglobin, promoting increased oxygen delivery to tissue

47
Q

The addition or removal of phosphate can cause…

A

reversible conformational changes in proteins

48
Q

The addition or removal of phosphate is a common form of

A

post-translational modification

49
Q

Protein kinases catalyse…

A

the transfer of a phosphate group to other proteins

50
Q

The terminal phosphate of ATP is…

A

transferred to specific R groups

51
Q

Protein phosphates catalyse the…

A

reverse reaction

52
Q

Phosphorylation brings about…

A

conformational changes, which can affect a protein’s activity

53
Q

The activity of many cellular proteins is regulated by…

A

phosphorylation

54
Q

Cellular proteins that are regulated by phosphorylation include…

A

enzymes and receptors

55
Q

Some proteins are activated by phosphorylation, while others are…

A

inhibited

56
Q

Adding a phosphate group adds…

A

negative charge

57
Q

Ionic interactions in the unphosphorylated protein can be…

A

disrupted and new ones created

AH Biology (31 decks)

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