Proteins Flashcards

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

Features and structures of fibrous proteins

A
  • formed from long insoluble molecules, due to high proportion of hydrophobic R-group amino acids
  • small amino acid range, with small R groups
  • repetitive primary structure amino acid sequence
  • make strong, long, complex molecules which AREN’T folded into 3D shapes
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Examples of fibrous proteins

A
  • elastin
  • keratin
  • collagen
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Function of elastin

A
  • found in elastic fibres within vessel walls and alveoli
  • flexible- allows expansion and return
  • quaternary protein made of stretchy molecules or tropoelastin
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Features of keratin

A
  • present in hair, skin, nails
  • large proportion of sulphur containing amino acids, resulting in strong, inflexible, insoluble materials
  • degree of bonds determines flexibility
  • unpleasant smell when burnt
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

structure of collagen, where found

A
  • connective tissue found in skin, tendons, ligaments
  • made of 3 polypeptides wound in a long, rope like structure
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Structure of globular proteins

A
  • compact
  • water soluble
  • roughly spherical
  • form when proteins fold into tertiary structures, and R groups kept away from aqueous environment
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Examples of globular proteins

A

insulin

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

function of insulin

A
  • hormone involved with blood glucose concentration
  • solubility and shape required
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Structure of conjugated proteins

A
  • globular proteins that contain a prosthetic group (a non protein component)
  • prosthetic groups lipids or carbs= glycoprotein, lipoprotein
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Examples of conjugated proteins

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

Function and structure of haemoglobin

A
  • oxygen carrying pigment in RBC
  • quaternary protein made of 4 polypeptides
  • 4 subunits, each containing a prosthetic haem group
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What is catalase

A
  • quaternary
  • enzyme= hydrogen peroxide breakdown
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What is a peptide

A
  • polymers made up of amino acid monomers
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What do proteins consist of

A
  • carbon, hydrogen, oxygen and nitrogen elements only
  • 1 polypeptide arranged as a complex macromolecule
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Amino acids- what is an R group, how many amino acids are there

A

-R group= variable groups, relative position and type determines the amino acid
- 20 different amino acids

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

How do amino acids join

A
  • amine and carboxylic acid groups react
  • the hydroxyl in the carboxylic acid group of 1 amino acid reacts with the hydrogen in the amine group of another amino acid
17
Q

What is a peptide bond

A
  • forms between 2 amino acids when they join
  • condensation reaction
  • results in a dipeptide
18
Q

What is a polypeptide

A
  • when many amino acids are joined
  • catalysed by enzyme peptidyl transferase
19
Q

How is a protein formed

A
  • different R groups interact with each other forming different types of bond which lead to long polypeptide chains folding into complex proteins
20
Q

What is the primary structure of a protein

A
  • the sequence in which the amino acids join
  • contained within DNA
  • Peptide bonds only
21
Q

What is the secondary structure of a protein

A
  • O, N, H atoms of amino acids interact
  • H bonds can form within an amino acid chain- pull it into a coil shape, ALPHA HELIX
  • Polypeptide chains can lie parallel to each other, patterns of each acid causes pleats= BETA PLEATED SHEET
  • secondary structure result of hydrogen bonds
22
Q

What is the tertiary structure of a protein

A
  • folding of the protein into its final shape
  • coiling/ folding brings different R groups closer to interact
  • interactions produce a variety of complex shaped proteins with specialised characteristics and functions
23
Q

What are the interactions between R groups

A
  • hydrophilic/ phobic reactions
  • hydrogen bonds
  • ionic bonds
  • disulfide bonds
24
Q

What is the quaternary structure of a protein

A
  • results from association of 2+ individual, different protein molecules (subunits)
25
Q

What enzyme breaks down peptide bonds into amino acids, type of reaction

A
  • proteases
  • hydrolysis (requires water)