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Biochemistry > Proteins > Flashcards

Proteins Flashcards

1
Q

What does contractile proteins do?

A

They permit movement in muscles

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2
Q

What do hemoglobin and albomin do?and where?

A

Transport molecules essential to life in the bloodstreams

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3
Q

What do immunoglobulins do?

A

Fight infectious bacteria and viruses.

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4
Q

What are the functions of aminoacids and proteins?

A

Direct and regulate metabolism,permit movement in muscles,incredible diversity of functions…

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5
Q

How are non standard aminoacids produced? Explain them.

A

Via chemical modification of standard aminoacids. Some Non standard aminoacids directly participate in building block of proteins.
Ornithine and citrulline in urea bio synthesis
Selenocysteine 21th aminoacid in glutathione peroxydase
6-n methyllysine in myosin

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6
Q

What are aminoacids made of? The structure

A

One carboxyl(coo)/primary alpha carbon group at the center/a distinctive R group side chain/an H
This structure is asymmetric

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7
Q

Do all aminoacids have stereoisomers? Give an example

A

Whole aminoacids have stereoisomers except glycine

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8
Q

What is physiological PH in aminoacids?

A

7,35-7,45 / carboxyl group(coo) is dissociated and Amino group is protonated

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9
Q

How are aminoacids found in mammalians?

A

Just found in L meaning left of the alpha carbon

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10
Q

In proteins are coo and NH3 available for chemical reactions?

A

Theyre not available for chemical reactions except for hydrogen and ionic bond formation

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11
Q

What are essential aminoacids?

A

Theyre necessary and indispensable and humans and other vertebrates cannot synthesize from metabolic intermediates

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12
Q

Name the essential aminoacids

A

MATTVILL => Methionine/Phenylalanie/Threonine/Tryptophan/Valine/Isoleucine/Leucine/Lysine

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13
Q

What are semi essential aminoacids? Name and explain them

A

Histidine and Arginine are semi essential amino acids and are essential at childhood.
Some adults may be able to synthesize Histidine on their own.

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14
Q

Name the classification of aminoacids.

A

Classification by R group/Chemical classification /Nutrutional classification /Metabolic classification

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15
Q

How is the classification of aminoacids by R groups?

A

To 2 kinds of polarity and shape.
For polarity it can be polar or non polar. The polar ones can be uncharged/positive/negative.
For the shape they divide into Aromatic and Aliphatic. Which the aromatic includes benzene ring and the aliphatic includes hydrocarbon CH3CH3 chain.

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16
Q

Name the R polar aminoacids.

A

1- OH => Serine, tyrosine , threonine
2- SH => Cysteine
3- Amide => Glutamine, aspargine
4- COOH => glutamic , aspartic
5- Nitrogen or NH2 => Lysine, Arginine, Histidine

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17
Q

What can R in polar aminoacids form?

A

Formation of hydrogen bond with H2O

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18
Q

Name Aromatic aminoacids.

A

We know theyre non polar and the examples are Phenylalanine and Tryptophan.

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19
Q

Which aminoacid contains ring with OH group?

A

So we can realize it is polar and the example is Tyrosine.

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20
Q

Name the nonpolar aminoacids.

A

Glycine/alanine/valine/leucine/isoleucine/phenylalanine/tryptophan/methionine/proline

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21
Q

Name an iminoacid

A

Proline

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22
Q

Name aliphatic hydrocarbons

A

They are nonpolar. Glycine/alanine/proline

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23
Q

Name branched chain hydrocarbons

A

They are non polar. Valine/leucine/isoleucine

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24
Q

Name a thioether group

A

Non polar . Methionine

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25
Q

Name an imidazole ring

A

It is polar. Histidine

26
Q

Name a guanidium group

A

It is polar. Arginine

27
Q

Name uncharged polar side chains

A

Cysteine/glutamine/aspargine/serine/threonine/tyrosine

28
Q

What is a buffer in aminoacids and how can it be created?

A

Both free aminoacids and some aminoacids can act as a buffer. They resist change in PH and can be created by mixing a weak acid and a conjugate base.

29
Q

How is zwitterion formed?

A

At neutral PH(7.4)

30
Q

What are glucogenic aminoacids?

A

Aminoacids converted into carbohydrates.

31
Q

Name Hromones derived from tyrosine

A

1-thyroid hormones such as T3 and T4
2- epinephrine and norepinephrine
3- Dopamine
4- Melanin

32
Q

From which aminoacid are niacin and serotonin derived?

A

They are both derived from tryptophan

33
Q

Give information about glutathione

A

A tripeptide found in most all organisms. Involved in protein and DNA sythesis,toxic substance metabolism and aminoacid transport
Glutamate,cysteine,glycine synthesize glutathione

34
Q

What is creatine derived from?

A

Glycine/arginine/methionine. (GAM code)

35
Q

What is hem derived from?

A

Glycine

36
Q

What is GABA derived from?

A

Glutamate

37
Q

What is histamine derived from ?

A

Histidine changes into histamine on decarboxylation.

38
Q

What do glycine and cysteine help in?

A

Synthesis of bile salts/detoxicants of specific substances

39
Q

Which aminoacids are used for pyrimidine and purine synthesis?

A

Pyrimidine => aspartate + glutamine
Purine => glycine + aspartic acid +glutamine + serine

40
Q

What are sources of sulphur?

A

Cysteine and methionine

41
Q

What are phosphorylated aminoacids?

A

An aminoacid residue is phosphorylated by a protein kinase by the addition of a covalent bond phosphate group.

42
Q

What is oxytocin?

A

A nanopeptide(9)/signal peptide / aids in uterine contraction/ejection of milk in mammals

43
Q

What is vasopressin?

A

Antidiuretic hormone,regulates water balance ,appetite,body temperature

44
Q

What is enkephalin?

A

It is a pentapeptide(5) found in saliva. There are two types of it we need to know:
1-methionine enkephalin useful energetic conditions
2- leucine enkephalin

45
Q

What is the protein structure ?

A

Primary: sequence of amioacids
Secondary: conformation and shape of backbone
Tertiary : 3D structure and interaction among R groups
Quaternary: if pr has more than one chain

46
Q

Give information about proteins secondary structure

A

It has two types of alpha helix and beta sheets.
Alpha helix is a hydrogen bonding between one peptide and the fourth one
Beta sheets is two or more peptides linked together by hydrogen bond(one chain and another chain)

47
Q

Which aminoacids can break the alpha helix in proteins secondary structure?

A

Glycine and proline

48
Q

Explain denaturation

A

Changing the structure of protein(alteration of the proteins shape) like heat/acids/bases/salts/mechanic agitation.
Primary structure cannot change due to denaturing.
Denaturing cannot absorb activation in cells

49
Q

Name classification of proteins

A

Two kinds of fibrous and globular
Fibrous => they are secondary structure only like collagens,elastins,keratins,myosins
Globulars => they are with three dimensional compact structures two kinds :
Albumins(egg whites) and globins(rich histidine)
Globulins such az y globin and enzymes

50
Q

What is the most abundant protein in human body?

A

Collagen

51
Q

Where is collagen?

A

They are fibrous proteins of the extracellular matrix found in skin/connective tissue /blood vessels /in the eye

52
Q

How many polypeptides does collagen have

A

3 a triple helix

53
Q

What is collagen rich in?

A

Glycine and proline. Glycine is the smallest aminoacid
Proline is essential for thermal stability

54
Q

What does collagen contain?

A

Hydroxyproline and hydroxylysine which arent present in most other proteins
So it has hydroxylation

55
Q

Give an example for post translation modification of collagen

A

Cofactors that are iron and vitamin c

56
Q

What do reactive aldehydes do with collagen?

A

Combines with collagen residues to form cross links

57
Q

Name important collagen types

A

Type I : dermis/bone/tendon /most collagen fibers of periodontium/collagen of PDL
Type II : cartilage/vitreous
Type III : blood vessels and seen in foetal tissues (janin)
Type IV : basement membranes/elastic system of gums
Type XI : cartilage
All of them are fibrillar except IV which is network

58
Q

Name two important collagen diseases.

A

Collagenopathies and genetic diseases.

59
Q

What is ehlers danlos syndrome?

A

It is an inheritable defect in the metabolism of collagen molecules. Symptoms such as skin extensibility and fragility and joint hypermobility.

60
Q

Explain osteogenesis imperfecta

A

Genetic disorder/brittle and fracture bone disease easily without trauma/most common mutation is replacement of glycine/abnomral alpha chains

61
Q

Explain dentinogenesis imperfecta

A

It is an important collagen disease most often blue-gray or yellow-brown. Teeth weaker than usual. It affects both primary and permanent teeth.

Biochemistry (3 decks)

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