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Topic 1 Biology > 1.3 Proteins > Flashcards

1.3 Proteins Flashcards

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1
Q

How do amino acids join?

A

they join together by a reaction between the amino group of one amino acid And the carboxyl group of another
They join in a condensation reaction and a molecule of water is lost

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2
Q

What is dipeptide

A

is two amino acids joined by a peptide bond

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3
Q

What is a peptide bond

A

The bond formed by a condensation reactions between amino acids

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4
Q

`What is a polypeptide bond

A

is a long chain of amino acids joined by peptide bonds

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5
Q

How is a protein formed

A

Proteins are formed in a condensation reaction when amino acid molecules join together and a water molecule is removed. The new bond formed in protein molecules where amino acids have joined

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6
Q

What is a disulfide bond

A

is a strong covalent bond formed as a result of an oxidation reaction between sulfur groups in cystine or methonince molecules which are close together in the strcuture of polypeptide

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7
Q

How do hydrogen bonds break

A

when the pH or temperature conditions change

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8
Q

How are hydrogen bonds formed

A

In amino acids, tiny negative charges are present on the oxygen and the carboyxl group
And
Tiny positive charges on the hydrogen atoms of the amino groups
When these charged groups are close together they attract
And a hydrogen bond is formed

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9
Q

Why are hydrogen bonds important

A

they are important in the folding and coiling of the polypeptide chains

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10
Q

Where can collagen molecules be found

A

fibrils

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11
Q

Where are collagen fibres found

A

They are found combined with the bone tissue, giving it tensile strength

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12
Q

Which strucutre(s) does globular proteins have

A

Complex tertiary and sometimes quaternary strucutre

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13
Q

What does globular proteins fold into

A

They fold into spherical (globular) shapes

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14
Q

Why do globular proteins molecules behave diffrently in water

A

Because their carboxyl and amino acids ends give them ionic properties

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15
Q

Instead of dissolving in water what do globular proteins form

A

Colloids

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16
Q

Why are globular proteins important

A

globular proteins form some enzymes and some hormones and involved in maintaining the structure of the cytoplasm

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17
Q

What is the strucurre of hameoglboin

A

Made up pf 574 amino acids
Arranged in four polypeptide chains which are held together by disulfde bonds

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18
Q

What ar econjugated proteins

A

protein that functions in interaction with other chemical groups attached by covalent bonding or weak interactions

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19
Q

What is a prosthtic group

A

Is the molecule that is incorporated in a conjugated protein

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20
Q

What is a glycoprotein

A

Is a protein with a carbohydrate prosthtihic group

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21
Q

Why are glycoproteins important

A

Glycoproteins acts a lubricant they are slippery and viscous and reduces friction

22
Q

What are lipoproteins

A

are proteins conjugated with lipids and are very important in the transport of cholestrol

23
Q

What is a primary struture

A

The linear sequnce of amino acids joined by peptide bonds`

24
Q

What is a secondary structure

A

The repeating pattern in the strucutre of the peptide chains such as A- helix or B- pleated sheets

25
Q

What is the tertiary strucutre

A

The three dimensional folding of the secondary structure

26
Q

What is the quaternary strutcure

A

the three dimensional arrangement of more that one tertiary polypeptide

27
Q

Why are disulfide bonds imporant

A

they are important for holding folded polypeptide chains in place

28
Q

What are salt bridges

A

ionic bonds can form between some of the strongly postive and negative amino acid side chains found buried deep in the protein molecules

29
Q

What is a fibrous protein

A

Are proteins that have long parallel polypeptide chains with occasional cross- linkages that form into fibres nit with little tertiary structure

30
Q

How many polypeptide chains is collagen made up of

A

3

31
Q

what type of structure of is collagen

A

Primary strucuture of these chains is repeating sequences of glycine with 2 other amino acids

32
Q

the 3 alpha chains in collagen

A

arragned in a unique triple helix held together by large number of hydrogen bond

33
Q

Strcuture of collagen

A

Primary strucutre with repeating sequences of glycine

the 3 alpha chains arrange into a triple helix held together by loads of hydrogen bond

34
Q

how is a peptide bond is formed

A

a bond forms between the carboxyl group of one amino acid and the amino group of a second amino acid

one water molecule is released

35
Q

What are the two common secondary structures of proteins?

A

Beta-pleated sheet
Alpha-helix

36
Q

What bonds are present in teriarty strucutre

A

Ionic bonds, hydrogen bonds , and displhuide bridges

37
Q

what are functions for globular proteins

A

Enzymes
Messengers

38
Q

What type of structure is found in globular proteins

A

Tertiary

39
Q

what is a conjugated protein?

A

specific type of globualr protein that contains a prosthetic group

40
Q

What are some similarities between hemoglobin and collagen

A

Both are polypeptides formed from amino acid monomers

Both have peptide bonds formed in condensation reactions

41
Q

What are differences between hb and collagen

A

Hemoglobin has a prosthetic hame group that contains iron to bond with oxygen, collagen has no prothesthic group.

hb is 4 pp chains collagen is 3 chains

hb is soluble, collagen is insoluble

42
Q

what do proteins contain

A

Hydrogen and oxygen they all contain nitrogen and many proteins also contain sulfur

43
Q

Why is the R group important

A

the structure of R group affects the way the AA bonds with other in the proteins

This depends if the r GROUP IS polar or not

44
Q

how do AA join

A

join together by a reaction between the amino group of one AA and the carboxyl group of another

45
Q

How is a protein formed q

A

when the polypeptide folds or coils or associates with other polypeptide chains

46
Q

Where does the peptide bond is formed

A

Between the OH of the carboxyl and the H of the amino group

47
Q

LABEL all fibrous protein properties

A

Insolubale
Hormones
Hydrophobic on the outside
Repeating AA sequnces

48
Q

LABEL or globualr protein properties

A

Soluable
Enzymes
Hydrophobic on the outside

-Little reption of AA sequences

49
Q

How des a change of AA lead to change in the structure and properties of a protein

A

Change in primary sequence
which leads to changed h bonds which affects the folding of the secondary strucutre

50
Q

describe dispuhlpoide bridges in hte tertiary strucuture of protiens

A

strong covlaent bonds between molecules of the AA cytecine

Topic 1 Biology (16 decks)

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