Unit 4 Test Two Flashcards Preview

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Flashcards in Unit 4 Test Two Deck (64)
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1
Q

What is primary structure

A

Sequence of amino acids in a polypeptide chain

2
Q

What is secondary structure

A

Hydrogen bonds are the hallmark in this type of structure

3
Q

What is tertiary structure

A

Stabilized by non covalent interactions and disulfide bonds

4
Q

What is quaternary structure

A

Subunits represent basic component

5
Q

What is a peptide bond

A

Linkage between the amino group of one amino acid and the carboxyl group of another amino acid

6
Q

What is alpha helix

A

Stabilized by H bonds between nearby amino acids (n+4) in a polypeptide chain

7
Q

What is motif

A

Super secondary structures in proteins

8
Q

Examples of helix breakers

A

Proline and glycine

9
Q

What are strong helix formers

A

Alanine and leucine

10
Q

What are some examples of beta turn formers

A

Proline and glycine

11
Q

What is a native fold

A

3D fold to fulfill specific biological function

12
Q

What are favorable interactions in proteins

A

Hydrophobic effect, h bonds, London dispersion, and electrostatic interactions

13
Q

What linkages are in primary structure

A

Covalent

14
Q

What linkages in secondary structure

A

H bonds

15
Q

What linkages in tertiary structure

A

Covalent, h bonds, ionic, van der waals, hydrophobic

16
Q

Linkages in quarternary structures

A

Same as tertiary

17
Q

What causes the peptide bond

A

Resonance

18
Q

What type of degradation uses phenyl isothiocyanate which labels N terminal amino acid

A

Edman degradation

19
Q

What reagent is used in edman degradation

A

Phenyl isothiocyanate

20
Q

Structure of globular proteins

A

Tertiary and quarternary

21
Q

Solubility of globular proteins

A

Fully soluble

22
Q

Functions of globular proteins

A

Dynamic

23
Q

Examples of globular protein

A

Hgb, myoglobin, enzymes

24
Q

Structure of fibrous proteins

A

Primary and secondary

25
Q

Solubility of fibrous proteins

A

Insoluble

26
Q

How to make fibrous proteins soluble

A

Break disulfide bonds

27
Q

Function of fibrous proteins

A

Structural, support

28
Q

Examples of fibrous proteins

A

Collagen, keratin and elastin

29
Q

Collagen contains what type of tripeptide sequence

A

Glycine x proline or glycine x 4Hyp

30
Q

Left or right handed collagen chain

A

Left

31
Q

Three alpha collagen chain, right or left handed

A

Right

32
Q

Making a triple helix in collagen helps what

A

Increase strength

33
Q

Prolyl hydroxylase and Lysyl hydroxylase requires what

A

O2, Fe and vitamin c

34
Q

What enzyme is needed for glycosylation of selected OH-Lys residues

A

Glucose or glucosyl-galactose

35
Q

What enzyme is needed for hydroxylation of selected pro and lys residues

A

Prolyl hydroxylase and lysyl hydroxylase

36
Q

The triple helix formation of pro collagen is what type of process

A

Spontaneous

37
Q

Cleavage of extension peptides requires what enzyme

A

Peptidases

38
Q

Assembly into microfibril is what type of process

A

Spontaneous

39
Q

Cross link formation to assemble collagen fibril contains what enzyme and other factor

A

Lysyl oxidase and copper

40
Q

Assembly into collagen fiber and aggregation of collagen fibers is what type of process

A

Spontaneous

41
Q

Type one of collagen genetic disease

A

Osteogenesis imperfecta which is weak bones. Mutation in type one collagen by replacing glycine with bulky side chain

42
Q

Type two collagen genetic disease

A

Chondriodysplasias which is abnormal cartilage, bone and joint deformities. Dwarfism

43
Q

Type three of collagen genetic diseases

A

Ehlers danlos syndrome. LETHAL, aorta rupture due to fragile skin and blood vessels

44
Q

Type 5 collagen genetic disorders

A

Ehlers danlos syndrome, hyper mobile joints, skin extensibility

45
Q

How does cross link formation occur in elastin

A

Lysyl side chains become delaminates by lysyl oxidase

46
Q

What is a desmosine and why important

A

Allysyl (3) and Lysyl side chain (1). This helps make elastin more stretchable

47
Q

Intrinsically disordered proteins purposes and score

A

Allows for conformation to bind to many different partner proteins and PONDR score shows probablity of interaction mostly and N and C terminus

48
Q

Proteins can be denatured by

A

Heat or cold, pH extremes, detergents, reducing agents and chaotropic agents

49
Q

What are chaotropic agents

A

Disrupt H bonds and denatures secondary structure

50
Q

What are examples of chaotropic agents

A

Urea and guanidinium hydrochloride

51
Q

Example of reducing agent

A

Beta mercaptoethanol

52
Q

What are examples of protein misfolding diseases

A

Alzheimers diseases, Parkinson’s disease, and Huntington’s disease, transmissible spongiform encephalopathies

53
Q

Common feature of amyloidosis

A

Missfolded proteins due to aggregation of B sheets

54
Q

How do prions spread

A

Prion protein attaches to healthy prion causing the alpha helices to turn into beta sheets

55
Q

What are Lewy bodies

A

Insoluble aggregates caused by a disorderly protein in the brain in Parkinson’s disease

56
Q

What activates pepsinogen

A

Hydrogen protons and pepsin

57
Q

Where is pepsinogen found

A

Stomach

58
Q

Pepsinogen targets what

A

Phenylalanine

59
Q

What activates trypsinogen

A

Enteropeptidase and trypsin

60
Q

Where is trypsinogen found

A

Pancreas

61
Q

What does trypsinogen target

A

Lysine and arginine

62
Q

What activates chymotrypsinogen

A

Trypsin and chymotrypsin

63
Q

What is the source for chymotrypsinogen

A

Pancreas

64
Q

What does chymotrypsinogen target

A

Aromatic and bulky amino acids