Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Science For Medicine JK > Proteins 1&2 > Flashcards

Proteins 1&2 Flashcards

You may prefer our related Brainscape-certified flashcards:
Biology 101 flashcards
1
Q

Aliphatic amino acids

A

Alkane/organic

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

Basic amino acid

A

Alkaline

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

Aromatic amino acids

A

Benzene

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

Other amino acid

A

Proline

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

Peptide bond

A

Formation of covalent bond with loss of water

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

Primary structure

A

Sequence of amino acids in polypeptide

Versatility in protein structure and function

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

Secondary structure

A

Spatial arrangement of amino acid residues near each other in linear sequence

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

Alpha helix

A

Held in place by hydrogen bonds

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

Beta pleated sheets

A

Hydrogen bonds between amide groups of linear polypeptide chain - porin

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

Tertiary structure

A

Spatial arrangement of amino acid residues that are far apart in a linear sequence

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

Examples of tertiary structure

A

hydrophobic interactions
Disulphide bridges
Van der waals
Hydrogen bonds

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

Ionic interactions

A

2 close oppositely charged R groups strong but rare

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

Van der waals

A

Non specific weak

Stabilise structure as strong together

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

Hydrogen bonds

A

Strong and permanent

1/20 strength of hydrogen bonds

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

Hydrophobic interactions

A

Intra polypeptide

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

Disulphide bridges

A

2 cysteine residues

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Quaternary structure

A

Spatial arrangement of individual polypeptide chains in a multi sub-unit protein
CRP - high when infected and haemoglobin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Denaturation - causes

A

Acids, heats, solvents, cross link reagents, chaotropic agents - molecule in water which disrupts bonds, disulphide bond reducers

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

What structures are effected by denaturation?

A

Secondary and tertiary

20
Q

What are the effects of denaturation

A
  • decreased solubility
  • loss of water binding capacity
  • Loss of biological activity
  • Improved digestibility
21
Q

Peptidases

A

Cleave peptide bonds

22
Q

Endopeptidase

A

Cleave internal bonds

23
Q

Exopeptidase

A

Cleave one amino acid at a time

24
Q

Carboxypeptidase

A

Cleave at COOH

25
Q

Aminopeptidase

A

Cleave at NH2

26
Q

What is protein structure dependent on?

A

DNA sequence

27
Q

Name 3 other types of proteins

A
  • glycoprotein
  • Lipoproteins
  • metalloprotein
28
Q

Glycoprotein

A

Protein and carbohydrate
post translational modification
Sugar binds to amino acid

29
Q

Example of glycoprotein

A

Antibody

30
Q

Roles of glycoproteins

A

cell recognition and signalling
Protein stabilisation
solubility

31
Q

Lipoprotein example

A

LDL, HDL

32
Q

Roles of lipoprotein

A

Transport water insoluble fats around the body

33
Q

Metalloprotein

A

1/3 of proteins - metal ion needed for activity

34
Q

Functions of metalloprotein

A

Transport
Enzyme
Storage
Signalling

35
Q

Globular proteins

A

Varied function including enzymes, hormones

36
Q

Fibrous proteins

A

Structural function eg tendon, connective tissue

37
Q

Membrane proteins

A

Cell/organelle proteins

Transporters and cell adhesion

38
Q

Co-operative binding

A

Binding at one subunit causes a change in shape of other subunits altering affinity for substrate

39
Q

Scurvy

A

Amino acid==>hydroxyamino acids
Weaker collagen
Acquired condition

40
Q

Osteogenesis imperfecta

A

Small glycine substituted for larger amino acid
Not as tight coil, reduced fibril interaction
Loss of secondary and tertiary structure
Weak and brittle collagen

41
Q

What is the main part of LDL

A

ApoB

42
Q

What internalises LDL?

A

Glycoprotein

43
Q

Where is LDL broken down?

A

Lysosomes

44
Q

Classes of effects and mutations in receptor

A
  • No receptor produced
  • Receptors never reach cell surface
  • Receptors cant bind LDL
  • Receptors don’t internalise on binding LDL
  • Receptors do not release LDL
45
Q

FH

A

Autosomal dominant

Mutation in LDL receptor

46
Q

Cryoglobulin

A

Proteins that precipitate in blood and solidify below 37 degrees which is a problem in extremities on a cold day

Science For Medicine JK (25 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions