Topic 1 - 1.24 Proteins :3 Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

what monomers are proteins made up of

A

amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

what are groups are amino acids made up of

A

Carboxyl group (-COOH), amino group(NH2) and an R group(either glycine which is -H or cysteine which is CH2-SH)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

what elements are proteins made of

A

nitrogen, oxygen, hydrogen, carbon and sometimes sulphur

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

How many naturally occurring amino acids are there

A

20

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

what is formed when 2 amino acids bond and what bond is formed

A

dipeptide, peptide bonds between carboxyl and amino acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

what other bonds except for peptide bonds can form between amino acids

A

depends on R group
disulfide, ionic and hydrogen bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Describe charges in an amino acid structure and how they help bonds form

A

the oxygen from the carboxyl group has a slightly negative charge while the hydrogen in the amino group has slightly positive charges.
this means they are attracted to eachother forming hydrogen bonds.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

when and how do disulfide bonds form

A

when 2 cysteine molecules (R group) in a polypeptide are close together
oxidation reaction between 2 sulphur containing groups… strong covalent bond knows as a disulfide bond.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

what protein structure are disulfide bonds usually present in

A

tertiary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What are salt bridges

A

ionic bonds between strongly positive and negative amino acid side chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Describe the primary structure of a protein

A

linear sequence of amino acids in a polypeptide

> > helps determine final 3 dimensional shape of the protein molecule

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Describe the Secondary structure of a protein

A

hydrogen bonds cause polypeptide to twist and fold into shape

examples-alpha helix or beta pleated sheets

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Describe the tertiary structure of a protein

A

3 dimensional shape of a polypeptide chain
first folds into secondary structure(hydrogen bonds)
chain continues folding into tertiary structure
active site of enzymes depends on tertiary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Describe the quaternary structure of a protein

A

the three dimensional arrangement of more than one tertiary polypeptide

> > > shows how individual sub units are arranged to form a larger 3 dimensional structure.

Also shows us the position of any prosthetic group

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Outline the structure of fibrous proteins and its properties

A

they have little/ no tertiary structure.
long parallel polypeptide chains, occasional cross linkages
insoluble in water+ very tough

found in connective tissue in tendons
keratin
matrix of bones

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

collagen is a fibrous protein outline its structure and properties for its function

A

made up of 3 polypeptide chains
primary structure= repeating sequences of glycine with 2 other amino acids(proline and hydro proline)
the 3 alpha chains are arranged in a unique triple helix held by hydrogen bonds

17
Q

what is osteogenesis imperfecta

A

collagen triple helix does not form properly therefore bone lacks tensile strength , therefore it is brittle and breaks easily

18
Q

What protein structure do globular proteins have

A

triple or quaternary

19
Q

what are conjugated proteins

A

protein molecules joined with a prosthetic group

20
Q

what prosthetic group to lipoproteins have and what properties does it give them

A

lipid phosphate group
important for the transport of cholesterol in the blood.
lipid part allows it to combine with the lipid cholesterol

21
Q

what prosthetic group do glycoproteins have and what properties does it give them

A

carbohydrate
helps them hold loads of water (slippery and viscous)and makes it harder for proteases to break them down

22
Q

identify 2 lipoproteins and their similarities/ differences

A

LDL-> low density lipoproteins
»>
HDL-> high density lipoproteins»> contain more protein than LDLs

23
Q

Test for proteins

A

Option 1. add 5% potassium or sodium hydroxide solution AND 1% (w/v) copper sulfate solution

Option 2. Biuret reagent (contains 2 chemicals above already mixed.) when reagent is added solution goes from blue to purple indicating the presence of protein