Proteins pt2 Flashcards

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1
Q

Amino acid sequence determines

A

protein structure

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2
Q

Proteins are polymers of

A

amino acid monomers

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3
Q

Amino acids link by __________ _____ to form polypeptides

A

peptide bonds

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4
Q

How are amino acids classified?

A

according to their R groups

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5
Q

basic amino acids are

A

positively charged

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6
Q

acidic amino acids are

A

negatively charged

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7
Q

All types of amino acid R groups

A

basic, acidic, polar, hydrophobic

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8
Q

The diversity of R groups result in

A

the wide range of functions carried out by proteins

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9
Q

What is the primary structure?

A

The sequence in which the amino acids are synthesised into the polypeptide

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10
Q

What results in regions of secondary structure?

A

Hydrogen bonding along the backbone of the protein strand

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11
Q

Examples of secondary structures

A

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

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12
Q

When the polypeptide folds into a tertiary structure this conformation is stabilised by

A

interactions between R groups: hydrophobic interactions; ionic bond; LDFs; hydrogen bonds; disulfide bridges.

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13
Q

Quaternary structure exists in proteins with

A

2 or more connected polypeptide subunits.

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14
Q

What is a prosthetic group?

A

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

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15
Q

Interactions of the R groups can be influenced by

A

temperature and pH

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16
Q

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

A

non-protein haem group

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17
Q

The charges on acidic and basic R groups are affected by

A

pH

18
Q

Key component of basic R group

A

NH2

19
Q

Key component of acidic R group

A

COOH

20
Q

Key component of polar R group

A

OH,NH3,SH

21
Q

Key component of hydrophobic (non-polar) R group

A

Hydrocarbon

22
Q

What is a ligand?

A

A substance that can bind to a protein

23
Q

R groups not involved in protein folding can

A

allow binding to ligands

24
Q

What happens as a ligand binds to a protein binding site?

A

The conformation of the protein changes. This change in conformation causes a functional change in the protein

25
Q

Where do allosteric interactions occur?

A

between spacially distinct sites

26
Q

Many allosteric proteins consist of

A

multiple units (have quaternary structure)

27
Q

Allosteric proteins with multiple subunits show cooperativity in binding in which

A

changes in binding at one sub-unit alter the affinity of the remaining subunits

28
Q

Allosteric enzymes contain a second type of site called

A

an allosteric site

29
Q

What do modulators regulate?

A

The activity of the enzyme when they bind to the allosteric site

30
Q

Following the binding of the modulator, what happens?

A

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

31
Q

The binding and release of oxygen in haemoglobin shows

A

cooperativity

32
Q

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

A

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

33
Q

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

A

substrate concentration.

34
Q

What do positive modulators do?

A

increase the enzyme’s affinity for the substrate

35
Q

What do negative modulators do?

A

reduces the enzymes affinity for the substrate

36
Q

Changes in binding of oxygen at one subunit

A

alter the affinity of the remaining subunits of oxygen

37
Q

What lowers the affinity of haemoglobin for oxygen so that the binding of oxygen is reduced

A

An increase in temperature or a decrease in pH

38
Q

What will reduced pH and increased temperature do to actively respiring tissue?

A

it will reduce the binding of oxygen to haemoglobin promoting increased oxygen delivery to tissue

39
Q

Adding a phosphate group adds

A

negative charges

40
Q

Ionic interactions in the unphosphorylated protein can be

A

disrupted and new ones added

41
Q

What do protein kinases do?

A

catalyse the transfer of a phosphate group to other proteins

42
Q

What do protein phosphatases do?

A

catalyse the reverse reaction (removes a phosphate group from a protein)