Brainscape's Knowledge GenomeTM

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


See full index

M2M unit 1 > Proteins > Flashcards

Proteins Flashcards

1
Q

Basic AA R groups

A

Can be protonated at physiological pH

Lysine, arginine, histidine

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

Spongiform Encephalopathy

A

Prp misfolds and caues other proteins to misfold

altered alpha helices to form beta sheets that cause them aggregate forms aggregates with amyloid plauques leading to neuronal loss and gliosis

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

What is the least hydrophobic of the non-polar AA?

A

Glycine

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

Cysteine

A

Cys C

Polar uncharged

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

what AA promote alpha helices?

A

hydrophobic Ala and Leu

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

Hsp70/Hsp40 in prokaryotes

A

prokaryoties are DnaK or DnaJ

bind to hydrophobic region to prevent aggregation

ATP hydrolysis

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

Sickle Cell Anemia

A

glutamine undergoes single amino acid change to make hemoglobin stickier and difficult to pass through capilary bed

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

what does alpha helices make

A

structural: keratin, myosin, fibrinogen
globlar: hemoglobin, myoglobin

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

Valine

A

Val V

Non polar aliphatic

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

How do aromatic groups absorb UV light?

A

at 280nm and its used to measure protein concentration. Absorbance is a function of concentration.

As concentration increases so does absorbance.

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

how does hemoglobin transport Co2?

A

CO2 is converted as Carbamate on amino terminal residues of hemoglobin

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

what AA promote Beta sheet formation

A

Trp, Ile, Val

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

DnaJ and DnaK

A

DnaJ binds to unfolded and facilitates DnaK binding.

DnaJ stimulates ATP hydrolysis by DnaK.

DnaK-ADP binds tightly to unfolded protein NT xchange factor stimulates release of ADP

ATP binds to DnaK to dissociate protein

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

What are the Aromatic AA?

A

hydrophobic as well as relatively non-polar

Phenylalanine, tyrosine, tryptophan

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

Isoleucine

A

Ile I

non-polar aliphatic

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

Beta turns

A

180 degree turn accomplished over 4 AA acids hydrogen bond between 1st A and 4th AA made

proline (2nd) or Glycine (3rd)

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

Relaxed Hemoglobin State

A

High affinity of O2 so when leaving the lungs it remains attached formation triggered by O2 binding.

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

Phenylalanine

A

Phe F

Aromatic R group

Hydrophobic least polar of the Aromatic group

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

Alpha helix

A

right hand screw

R groups pointing outward bond

between every 5 residues Carbonyl O and amine

Inner diameter is too small out

diameter fits in major groove of DNA

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

Aliphatic side chains - meaning

A

carbons in open chain conformation

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

Amyloidosis

A

generalized protein misfolded in rest of body leading to variety of disease (T2D to cardiac amyloidosis)

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

Lysine

A

Lys K Polar Basic (positively charged) pKa 10

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

L Isomer vs D isomer

A

L: with hydrogen backwards is CORN counterclockwise D: with hydrogen backwards is CORN clockwise All amino acids have L isomers

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

what is the signficance of 1 and 8 lining up in alpha helces

A

allows the formation of a leucine zipper

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

Serine

A

Ser S Polar, unchraged

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

Acetyl modificaiton

A

occurs on lysine, especially on histones

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

y-caroxyglutamate

A

A blood clotting prothrombin protein

Vitamin K added

carboxyl group

Warfarmin (Coudamin) prevents blood clotting

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

Tyrosine

A

Tyr T

Aromatic R Group hydrophobic and slightly polar (not really) can form H bonds

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

Triple Helix

A

rich in glycine and proline

rich in turns and loops, but proline are hydroxylated via vitamin C

allows massive H bonding E

very third residue is glycine in collagen

30
Q

Chaperonin

A

a cap and 2 7 subunit rings in prok GroEL and GroES required for 10-15% coupled to ATP hydorlysis and conformational changes

31
Q

Alanine

A

Ala A non-polar Aliphatic

32
Q

Collagen

A

tensile strength, non-stretching tendons, cartilage, bones, cornea long

glycine and proline rich

Super helical triple helix higher tensile strength than steel wire.

33
Q

Gel Filtration Chromatography

A

Purify proteins according to size Proteins run through filtration column large flow faster and small slower

34
Q

what happens with pH>pKa

A

deprotonated base form denominates

35
Q

What AA are non-polar, aliphatic

A

Glycine, alanine, valine, leucine, methionine, isoleucine

36
Q

Why does Myoglobin use heme?

A

\generate free radicals

heme not generate free radicals!

myoglobin cant bind to O2 itself

37
Q

Edman Degredation

A

label and remove N terminal AA one at a time and identify

38
Q

Tense Hemoglobin site

A

Lower binding affinity so in high O2 region of lungs, O2 will bind very easily

39
Q

Protein Prolyl Isomerase

A

Reforms proline from Trans to the cis

formation cis is important in Beta turns

40
Q

Alpha Keratin

A

tough rigid, hard materials in nails and horns

cross linked alpha helices and S-S rich in hydrophobic residues form by alpha helices that coil together to form a coiled coil (left) to combine in a protofilmant and a protofibril and intermediate filament

41
Q

Bortezomib

A

takes advantage of cancer cells always proliferating and proteasome is in high demand. acts on proteasome inhibitor and this has more pronounced effect on cancer cells. treats multiple myeloma

42
Q

Methylation Modification

A

Occurs on lysine or arginine can have 1, 2, or 3 methyl groups methylation of histones

43
Q

what aa do not promote beta sheet formation

A

Pro Gly

44
Q

Polar R Group AA

A

Serine, Threonine, Cysteine, Asparagine, Glutamine

45
Q

Disulfide Isomerase

A

correct disulfide bond formation between free cysteines especialy important when there are many free cysteines done on secreted of cell surface proteins

46
Q

Leucine

A

Leu L non polar aliphatic

47
Q

Tryptophan

A

Trp, W Aromatic R group Hydrophobic and slightly polar

48
Q

Ion Exchange Chromatography

A

purify proteins according to charge run through cation exchange resin column with negatively charged beads. Positive charged particles stick and can be eluted with salt

49
Q

Isoelectric Point

A

point at which the pH at which the protein carries equal number of + and - charge. pI is essentially pKa value pI > pH = positive charged (lysozyme) pI

50
Q

Arginine

A

Arg, R Polar Basic (positively charged) pKa 12

51
Q

Histidine

A

His, H Polar Basic (positively charged) pKa 6.5

52
Q

Hydroxyproline

A

found in collagen and CT

Addition of OH group onto proline is responsible for strength

Facilitated by Vitamin C *Scurvy*

53
Q

Slk Fibroin

A

soft, flexible fiber held together by Beta sheet and van der waals intercations

54
Q

Immunoglobulin

A

one heavy chain composed of 4 beta sheets one ligh chain composed of 2 beta sheets dimers antigen binding domain

55
Q

Asparagine

A

Asn N Polar, uncharged

56
Q

Proline isomers

A

most peptide bonds are in trans conformation, but proline has 6% are in cis

57
Q

Methionine

A

Met, M non-polar aliphatic

58
Q

Histamine

A

formed from the removal of CO2 from histidine

59
Q

Gleevec

A

tyrosine kinase inhibitor that treats chronic myelogenous leukemia binds to bcr-abl fused protein to inhibit the kinase

60
Q

Asparate

A

Asp D Polar Negative (acid) pKa 4.4

61
Q

Acidic AA R groups

A

Asparate and Glutamate Deprotonated at physiological pH

62
Q

O linked vs N linked glycosylation

A

O: sugars added to Ser and Thr N linked: sugars added to Asp in sequnes XNX-S/T

63
Q

Bohr effect

A

pH difference in lung vs tissue to increase O2 transfer

64
Q

what AA do not promote alpha helices?

A

proline and glycine

65
Q

how is hemoglobin influenced by pH

A

blood in lungs have higher pH than blood, O2 binds better PH in tissue is lower, thus O2 is released

66
Q

Thryoid hormone

A

L-thyroxin is formed by modification of tyrosine

67
Q

ALB protein

A

ALB is a kinase that normally phosphorylates and dephosphorylates as regulatory protein. When fused with BCR, it is always active and leads to continuous phosphorylation - thus leukemia.

68
Q

what is scurvy caused by?

A

lack of vitamin C

Proline does not get hydroxylated so

4-hydroxyproline is not formed

69
Q

Glutamine

A

Gln, Q polar, uncharged

70
Q

Glutamate

A

Glu E Polar Negative (acid) pKa 4.4

71
Q

Threonine

A

Thr, T polar uncharged

72
Q

Kd

A

[p][L][pL] dissociation constant when Kd is higher, binding strength is low when Kd is low, binding strenth is high

M2M unit 1 (6 decks)

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