Brainscape's Knowledge GenomeTM

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


See full index

Bio Chem > Proteins > Flashcards

Proteins Flashcards

You may prefer our related Brainscape-certified flashcards:
Periodic Table flashcards Chemistry 101 flashcards AP® Chemistry flashcards Biology 101 flashcards Organic Chemistry 101 flashcards
1
Q

Proteins have more … than NA

A

Structural diversity

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

How many a.a in long protein

A

100

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

What is the pl equation at equivalence point

A

pI = (pK1 + pK2)/2

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

Pl for acidic acid (D,E)

A

pI = (pK1 + pKR )/2

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

Pl for basic aa (k,r,h)

A

pI = (pK2 + pK2 )/2

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

Do proteins have high or low stability at ph=pl

A

Low stability and leads to precipitation

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

What does isoelectric separating use

A

Pl difference

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

What are the 10 amino acids

A

F, V, W, T, I, M, H, R, K, L

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

How are peptide bonds formed?

A

Reaction of nh2 and cooh from aa

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

What are the structure of peptide bonds

A

Linear from one aa to another

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

Where are the peptide bonds synthesized

A

N terminus -> C terminus

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

What two polypeptide chains are joined by disulfide bonds

A

A and B

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

Does the bond have a full or partial bond

A
  1. Partial double bond character
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Is there rotation around the peptide bond

A

No

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

Where is the point of flexibility along the backbone

A

Alpha carbon

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

What describes the secondary conformation along the backbone

A

Psi and pi

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

Chiral compounds are…

A

Optically active

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

Chiral compounds rotate the …

A

Plane of polarized light

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

All aa are chiral except

A

Glycine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

In a racemic how many are optically active

A

50:50

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

What degree of rotation in a racemic

A

Zero rotation of plane-polarized light

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Primary structure

A

Aa sequence of protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Secondary structure

A

Hélix, sheet, turn/loop

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Tertiary structure

A

Folded structure of whole protein ( s-s bonds)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

Quarternary

A

Assembled complete ( oligomer)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

What helices fits in the major groove of dsDNA and recognizes specific dna sequence and bind to it via h-bonds

A

A-hélices

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

What type of aa are in the central regions

A

Hydrophobic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

What are the two types of beta sheets

A

Parallel and antiparallel

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

What do the two beta sheets have in common

A

Inter-strand h-bonding between c=o and n-h

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

What are the differences in the beta sheets

A

Length of the loop( may contain alpha helical segments) and the direction of the associated b strand

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

What form of sheets can transport things

A

Beta sheets

32
Q

Beta sheets fit into … grooves

A

Minor

33
Q

What is a beta barrel

A

Twisted and inclined beta sheet

34
Q

What causes diff types of turns in secondary proteins

A

Different number of residuals and h-bonding patterns

35
Q

What joins other 2 degree structures in beta parallel sheets

A

Loops

36
Q

Type 1 beta turn

A

R group on the same side

37
Q

Type 2 beta turn

A

R groups on the opposite sides

38
Q

What aa is used in y-turns

A

Proline

39
Q

In a domain what is on the inside and outside

A

Hydrophobic: hydrophilic

40
Q

How are proteins in quarternary structure stabilized

A

Non covalent interactions of the r groups and can be stabilized by covalent s-s bonds

41
Q

What part of the body has alpha keratin

A

Hair, nails, and part of the skin

42
Q

What is a monomer

A

Long alpha helix

43
Q

What residue is hydrophobic in a monomer

A

4th residue

44
Q

What is a coiled-coil dimer stabilized by

A

Hydrophobic interactions

45
Q

What way do pair of helices wind

A

Left- hand fashion

46
Q

What is there a large number of in alpha structures

A

Cysteine

47
Q

What repeats in beta sheets

A

Glycine and alanine and serine

48
Q

Layers of beta sheets lead to what

A

Toughness and flexibility

49
Q

Keratin is very

A

Strong and flexible cable-like structures

50
Q

Fibrous protein are … in water

A

Insoluble

51
Q

Globular proteins are … in water

A

Soluble

52
Q

What are orthologs

A

-Similar seq found in different species
- conventional divergence ( specification)

53
Q

What are paralogs

A

-Similar seq found in the same species
- gene duplication

54
Q

…kill nerve cells

A

Protein aggregates

55
Q

Protein misfolding is…

A

Spontaneous

56
Q

Myoglobin and hemoglobin structure

A

Monomer; tetramer

57
Q

Myoglobin and hemoglobin binds to:

A

1 o2: 4 o2

58
Q

What are the affinities for myoglobin and hemoglobin

A

High; moderate

59
Q

What are the functions of myoglobin and hemoglobin

A

Store; transport

60
Q

Sensitivity to ph for myoglobin and hemoglobin

A

Unaffected by ph; sensitive to ph

61
Q

Function of hsp

A

Assist folding

62
Q

What type of residue are associated with hsp

A

Hydrophobic

63
Q

What is zymogen

A

Catalytically inactive protein precursor

64
Q

What does low p50 mean

A

High o2 affinity

65
Q

What curve is very efficient in o2 transport

A

Sigmoidal o2 binding curve

66
Q

What is Cooperactivity

A

Filling 1st heme sites which lead to affinity of the other sites for o2

67
Q

Does heme cause structural change?

A

Yes, the binding of o2 with iron pull on helix F causing a change

68
Q

What factors affect o2 affinity

A

BPG
Low ph
Co2 from tissues
Temperature increase

69
Q

Mutation in which residue causes sickle cell

A

Glycine-> valine

70
Q

What is the first step in precipitation and diff solubilization

A

Precipitation with salts like nh4, so4

71
Q

What is the purpose of the edamame degradation

A

Identify the n-terminal amino acid of a polypeptide

72
Q

What gels are used in gel filtration

A

Porous gels: separate small, denatured or solubilized proteins

73
Q

Which proteins elute first and last

A

Larger proteins; smaller ones

74
Q

How is Ion exchange chromatography column selected

A

Type and strength of charge

75
Q

What is the elution order

A

Weakly charged-> moderate-> strongly- charged

76
Q

Affinity chromatography is separated by

A

Molecular conformation

77
Q

What uses antibodies to detect specific proteins

A

Elisa and western blotting

Bio Chem (3 decks)

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