Proteins pt2 Flashcards

(42 cards)

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

18
Q

Key component of basic R group

19
Q

Key component of acidic R group

20
Q

Key component of polar R group

21
Q

Key component of hydrophobic (non-polar) R group

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
Where do allosteric interactions occur?
between spacially distinct sites
26
Many allosteric proteins consist of
multiple units (have quaternary structure)
27
Allosteric proteins with multiple subunits show cooperativity in binding in which
changes in binding at one sub-unit alter the affinity of the remaining subunits
28
Allosteric enzymes contain a second type of site called
an allosteric site
29
What do modulators regulate?
The activity of the enzyme when they bind to the allosteric site
30
Following the binding of the modulator, what happens?
The conformation of the protein changes and this alters the affinity of the active site for the substrate
31
The binding and release of oxygen in haemoglobin shows
cooperativity
32
The binding of a substrate molecule to one active site of an allosteric enzyme...
increases the affinity of the other active sites for binding of subsequent substrate molecules.
33
The activity of allosteric enzymes can vary greatly with small changes in
substrate concentration.
34
What do positive modulators do?
increase the enzyme's affinity for the substrate
35
What do negative modulators do?
reduces the enzymes affinity for the substrate
36
Changes in binding of oxygen at one subunit
alter the affinity of the remaining subunits of oxygen
37
What lowers the affinity of haemoglobin for oxygen so that the binding of oxygen is reduced
An increase in temperature or a decrease in pH
38
What will reduced pH and increased temperature do to actively respiring tissue?
it will reduce the binding of oxygen to haemoglobin promoting increased oxygen delivery to tissue
39
Adding a phosphate group adds
negative charges
40
Ionic interactions in the unphosphorylated protein can be
disrupted and new ones added
41
What do protein kinases do?
catalyse the transfer of a phosphate group to other proteins
42
What do protein phosphatases do?
catalyse the reverse reaction (removes a phosphate group from a protein)