Brainscape's Knowledge GenomeTM

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


See full index

Biology > Proteins > Flashcards

Proteins Flashcards

1
Q

All enzymes are ____

A

Proteins

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

Proteins are also essential in cell membrane:they act as ____ & ______

A

receptor proteins
signaling proteins

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

Some hormones are proteins eg._____ and _____

A

insulin
glucagon

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

Proteins that functions as oxygen-carrying pigments

A

hemoglobin-carry oxygen to blood
myoglobin-carry oxygen to muscle

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

Proteins also have defensive functions.
True or False?

A

True
antibodies are proteins

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

What are structural proteins?

A

Collagen-bone and walls of arteries
Keratin-hair,nail,skin

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

Proteins for muscle contraction

A

Actin
Myosin

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

What are storage protein?

A

milk
egg white

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

Monomers of proteins are ____

A

amino acids

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

Amino acids contains ____,______,_____ and _____

A

Amine gp (NH2)
Carboxylic acid gp (COOH)
Hydrogen
Functional R group

20 amino acids only differ in R gp

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

How polypeptides formed?

A

When many amino acids are joined by PEPTIDE BOND

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

Peptide bond is formed by ____ reaction

A

condensation

COOH gp lose OH and NH2 gp lose H—>H2O

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

What is protein?

A

functional molecule made up of 2 or more polypeptides

(polypeptides ကိုfunctional proteinsဖြစ်အောင်fold လုပ်ထား)

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

Protein function depends on _____

A

R group nature
-nonpolar R gp—->Hydrophobic
-polar R gp——>Hydrophilic
-negative charge—->Acidic
-positive charge——>Basic

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

Polypeptides can be broken down into amino acids by ____ reaction

A

hydrolysis

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

Why polypeptide chain have 2 terminal?

A

one end of the chain has NH gp and the other end has COO gp also known as amino terminal(N-terminal) and carboxyl terminal(C-terminal)

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

All proteins have quaternary structure.
True or False?

A

False
Proteins containing 2 or more polypeptides chain can formed quaternary structure.

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

What is primary structure of protein?

A

linear chain of amino acids
Joined by PEPTIDE BOND

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

Types of protein

A

1)Globular protein-spherical
2)Fibrous protein-long fibers

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

What is secondary structure of protein?

A

Polypeptide chains contains many N-H bond(Hမှာpartial positive charge) and C=O bond( Oမှာ partial negative charge) ——>forming HYDROGEN BOND

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

Types of polypeptide chain

A

1)alpha helix
2)Beta pleates
3)Beta turn
4)Omega loop

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

What is the alpha helix?

A

Polypeptides chain coiled by formed HYDROGEN BOND

(1st amino acidမှာရှိတဲ့NH gpက4th amino acidမှာရှိတဲ့ CO gpနဲ့join)

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

What is difference b/w right-head helix and left hand helix?

A

-right-hand helix—>clockwise
They are stable but less energy

-left-hand helix—->counterclockwise
They are less stable but more energy

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

How beta-pleated sheet formed?

A

when parallel segments of polypeptide chains joined by HYDROGEN BOND

-antiparallel—>an amino acid joined to an amino acid

-parallel——>an amino acid is joined to two other amino acid

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

How beta turn is formed?

A

Polypeptide chain is turned and joined by HYDROGEN BOND

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

How tertiary structure formed?

A

R gp of polypeptide chains joined by weak interaction (aka hydrophobic interactions)

Nonpolar R gp at the core of protein and polar R gp at the outside

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

Bonds formed in tertiary structure

A

-nonpolar R gp are joined by Van der Waals force
-polar side chain are joined by hydrogen bond
-charged side chain are joined by ionic bond
-sulfur containing side chains are joined by disulfide bridge

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

R gp of hemoglobin is ____

A

heme gp containing iron atom

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

How quaternary structure formed?

A

QUATERNARY structure only formed when there is 2 or more polypeptide chains

Quaternary structure is aggregation of these polypeptide chains

30
Q

What is structural difference b/w hemoglobin and myoglobin?

A

Hemoglobin have quaternary structure but myoglobin does not have quaternary structure.

**Hemoglobin-4 polypeptide
**Myoglobin-1 polypeptide

31
Q

Features and functions of Globular protein

A

-spherical shape
-soluble in water

Func:metabolic reactions (such as transport protein,enzymes and hormones)
eg.hemoglobin,myoglobin,insulin,lipase

32
Q

Features and Function of Fibrous protein

A

-long fiber
-insoluble
-tensile strength

Func:structural role(eg. collagen and keratin)

33
Q

Polypeptides chain in hemoglobin

A

2 alpha chain (made from alpha globin)
2 beta chain (beta globin)

34
Q

Is the polypeptide chains of hemoglobin identical?

A

No

Hemoglobin is heterotetromer (different 4 polypeptide chain)

35
Q

When protein contains 2 subunit,it is called ____

A

dimer

36
Q

Hemoglobin can carry _____ oxygen

A

4 molecules of oxygen
(heme gpလေးခုပါ ironလေးလုံးနဲ့O2 လေးလုံးပေါင်း)

37
Q

What is the color of blood when hemoglobin is binds to oxygen?

A

Bright red

compound:oxyhemoglobin

38
Q

What is the color of blood when hemoglobin is not bound to oxygen?

A

purplish

39
Q

Collagen contains ____ subunit and ____ shape

A

3
helical shaped

Collagen is trimer

40
Q

Three strands of polypeptide is bound by _____

A

HYDROGEN BOND

collagen ရဲ့third amino acid ကglycine (အသေးဆုံးa/aမလို့ collagen ကcompactဖြစ်)

41
Q

What is the structural difference b/w hemoglobin and collagen?

A

Hemoglobin has tertiary structure and collagen doesn’t have

42
Q

Most proteins denature if they transferred from aqueous environment to _____ solvent

A

nonpolar

(nonpolr solventနဲ့ပေါင်းဖို့hydrophobic regionတွေကအပြင်ကိုထွက်သွားလို့)

43
Q

What is sickle cell disease ?

A

genetic blood disorder

44
Q

Sickle cell disease is caused by _____

A

change in amino acid sequence of primary structure

(6th amino acidမှာ glutamic acid(polar)အစား valine(nonpolar)ဖြစ်သွား)

45
Q

What is shape of RBC in normal hemoglobin and sickle cell?

A

normal hemoglobin-biconcave shaped
sickle cell-sickle shaped

46
Q

Denaturation can caused by

A

pH,temp,chemical and enzymes

47
Q

Denatured proteins are biologically ____

A

inactive

48
Q

Denaturation is reversible or not?

A

Sometimes reversible but mostly irreversible

49
Q

Denaturation of globular protein can cause _____

A

insoluble and inactive

50
Q

Denaturation of fibrous protein can cause _____

A

less structural strength

51
Q

Increasing in temperature can destroy ____ structures

A

secondary
tertiary
quaternary

BY BREAKING H BOND

52
Q

Changes in pH can destroy _____ structures of protein

A

tertiary
quaternary

BY BREAKING IONIC BOND

53
Q

Changes in chemical can destroy _____ structures of proteins

A

secondary
tertiary
quaternary

BY BREAKING H BOND

54
Q

Enzymes can destroy ____ structures of protein

A

all structures of protein even primary structure

55
Q

Basic structure of protein

A

R
|
NH2-C-COOH
|
H

Amino acid

56
Q

What interactions are between the secondary structures of proteins?

A

Hydrogen bonding between the amino group and carboxyl group

Alpha and beta pleated

57
Q

What bonds are between tertiary structure of proteins

A

Ionic bonds, salt bridges, hydrophobic interaction and disulphide
linkages between R groups.

58
Q

What is quantenary structure

A

Two or more ploypeptide chains into a single functional unit.

Insulin- heterodimer Collagen-homotrimer Haemoglobin-heterotetramer

59
Q

How many kinds of shapes do proteins have?

A

Globular shapes- ( water soluble)- hydrophobic R groups inside,a hydrophilic R groups inside eg- haemoglobin

Fibrous shapes- water insoluble - have structural roles. Eg- collagen

60
Q

What are 20 common amino acids that make up proteins?

A

ALL HIS TV MPT

Arginine
Leucine
Lysine
Histidine
Isoleucine
Threonine
Valine
Methionine
Phenylalanine
Tryptophan

61
Q

What kind of amino acid is an exception to standard amino acid?

A

Proline because R group is not separated from amino group.

62
Q

How are peptide bonds formed between amino groups in proteins?

A

By condensation reaction/ dehydration synthesis reaction

Removal of OH group from COOH and Removal of H from NH2-removal of water

63
Q

What happens when amino acid loses their 3D structure?

A

Loses their function

Protein denaturation- primary structure of the protein sequence is not lost

64
Q

What can misfolding of proteins lead to?

A

Misfolding of proteins can lead to serious diseases such s Parkingson’s , Alzheimer’s and mad cow diseases

65
Q

What is unique to the structure of insulin?

A

Contains two polypeptide chain A and B 21 and 30 amino acids respectively

A chain’s N terminal = glycine
C terminal = asparagine

66
Q

Why does sickle cell anaemia occur?

A

One amino acid which occurs at the beta chain is replaced by another amino acid
Glutamate is replaced by valine, which is non polar. Having a non polar R group on the outside of the molecule makes the haemoglobin much less soluble. And crescent shaped sickle cells appear, by preventing blood flow to organs, dizziness, headaches, breathlessness occurs.

67
Q

What kind of mutation is the sickle cell anaemia mutation

A

Point mutation. Haemoglobin has 2 alpha subunits and alpha subunits. Each globin chain has 150 amino acids. Each amino acid is coded by three codons.
Therefore= 15043= 1800

A single nucleotide mutation 1 in 1800

68
Q

Haem group in haemoglobin carries oxygen and it is not made with proteins, what is it called?

A

Prosthetic group

69
Q

Which molecules assist protein folding?

A

Chaperones

70
Q

Can denaturation be reversible?

A

Yes, in some proteins, after removing denaturation agents, the proteins func can be restored, but in others, it is permanent

71
Q

Does high temp and acidic pH always lead to denaturation?

A

No, some bacteria in hot living springs and stomach enzymes are still surviving

72
Q

What proteins are soluble; globular or fibrous?

A

Globular are soluble

Biology (16 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions