Brainscape's Knowledge GenomeTM


Top Flashcards (Certified)
All Flashcards

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
How beta turn is formed?
Polypeptide chain is turned and joined by HYDROGEN BOND
26
How tertiary structure formed?
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
27
Bonds formed in tertiary structure
-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
28
R gp of hemoglobin is ____
heme gp containing iron atom
29
How quaternary structure formed?
QUATERNARY structure only formed when there is 2 or more polypeptide chains Quaternary structure is aggregation of these polypeptide chains
30
What is structural difference b/w hemoglobin and myoglobin?
Hemoglobin have quaternary structure but myoglobin does not have quaternary structure. **Hemoglobin-4 polypeptide **Myoglobin-1 polypeptide
31
Features and functions of Globular protein
-spherical shape -soluble in water Func:metabolic reactions (such as transport protein,enzymes and hormones) eg.hemoglobin,myoglobin,insulin,lipase
32
Features and Function of Fibrous protein
-long fiber -insoluble -tensile strength Func:structural role(eg. collagen and keratin)
33
Polypeptides chain in hemoglobin
2 alpha chain (made from alpha globin) 2 beta chain (beta globin)
34
Is the polypeptide chains of hemoglobin identical?
No Hemoglobin is heterotetromer (different 4 polypeptide chain)
35
When protein contains 2 subunit,it is called ____
dimer
36
Hemoglobin can carry _____ oxygen
4 molecules of oxygen (heme gpလေးခုပါ ironလေးလုံးနဲ့O2 လေးလုံးပေါင်း)
37
What is the color of blood when hemoglobin is binds to oxygen?
Bright red compound:oxyhemoglobin
38
What is the color of blood when hemoglobin is not bound to oxygen?
purplish
39
Collagen contains ____ subunit and ____ shape
3 helical shaped Collagen is trimer
40
Three strands of polypeptide is bound by _____
HYDROGEN BOND collagen ရဲ့third amino acid ကglycine (အသေးဆုံးa/aမလို့ collagen ကcompactဖြစ်)
41
What is the structural difference b/w hemoglobin and collagen?
Hemoglobin has tertiary structure and collagen doesn’t have
42
Most proteins denature if they transferred from aqueous environment to _____ solvent
nonpolar (nonpolr solventနဲ့ပေါင်းဖို့hydrophobic regionတွေကအပြင်ကိုထွက်သွားလို့)
43
What is sickle cell disease ?
genetic blood disorder
44
Sickle cell disease is caused by _____
change in amino acid sequence of primary structure (6th amino acidမှာ glutamic acid(polar)အစား valine(nonpolar)ဖြစ်သွား)
45
What is shape of RBC in normal hemoglobin and sickle cell?
normal hemoglobin-biconcave shaped sickle cell-sickle shaped
46
Denaturation can caused by
pH,temp,chemical and enzymes
47
Denatured proteins are biologically ____
inactive
48
Denaturation is reversible or not?
Sometimes reversible but mostly irreversible
49
Denaturation of globular protein can cause _____
insoluble and inactive
50
Denaturation of fibrous protein can cause _____
less structural strength
51
Increasing in temperature can destroy ____ structures
secondary tertiary quaternary BY BREAKING H BOND
52
Changes in pH can destroy _____ structures of protein
tertiary quaternary BY BREAKING IONIC BOND
53
Changes in chemical can destroy _____ structures of proteins
secondary tertiary quaternary BY BREAKING H BOND
54
Enzymes can destroy ____ structures of protein
all structures of protein even primary structure
55
Basic structure of protein
R | NH2-C-COOH | H Amino acid
56
What interactions are between the secondary structures of proteins?
Hydrogen bonding between the amino group and carboxyl group Alpha and beta pleated
57
What bonds are between tertiary structure of proteins
Ionic bonds, salt bridges, hydrophobic interaction and disulphide linkages between R groups.
58
What is quantenary structure
Two or more ploypeptide chains into a single functional unit. Insulin- heterodimer Collagen-homotrimer Haemoglobin-heterotetramer
59
How many kinds of shapes do proteins have?
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
What are 20 common amino acids that make up proteins?
ALL HIS TV MPT Arginine Leucine Lysine Histidine Isoleucine Threonine Valine Methionine Phenylalanine Tryptophan
61
What kind of amino acid is an exception to standard amino acid?
Proline because R group is not separated from amino group.
62
How are peptide bonds formed between amino groups in proteins?
By condensation reaction/ dehydration synthesis reaction Removal of OH group from COOH and Removal of H from NH2-removal of water
63
What happens when amino acid loses their 3D structure?
Loses their function Protein denaturation- primary structure of the protein sequence is not lost
64
What can misfolding of proteins lead to?
Misfolding of proteins can lead to serious diseases such s Parkingson’s , Alzheimer’s and mad cow diseases
65
What is unique to the structure of insulin?
Contains two polypeptide chain A and B 21 and 30 amino acids respectively A chain’s N terminal = glycine C terminal = asparagine
66
Why does sickle cell anaemia occur?
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
What kind of mutation is the sickle cell anaemia mutation
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= 150*4*3= 1800 A single nucleotide mutation 1 in 1800
68
Haem group in haemoglobin carries oxygen and it is not made with proteins, what is it called?
Prosthetic group
69
Which molecules assist protein folding?
Chaperones
70
Can denaturation be reversible?
Yes, in some proteins, after removing denaturation agents, the proteins func can be restored, but in others, it is permanent
71
Does high temp and acidic pH always lead to denaturation?
No, some bacteria in hot living springs and stomach enzymes are still surviving
72
What proteins are soluble; globular or fibrous?
Globular are soluble

Biology (16 decks)

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