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Chapter 2- nucleic acids and proteins > 2A > Flashcards

2A Flashcards

protein structure and function

1
Q

Protein/polypeptide

A

diverse group of moleculesMade of monomers of amino acids bound together via peptide bonds and has several structural and functional properties like hair and bodily processes.

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2
Q

what is DNA made of

A

Dna contains a phosphate gorup, a 5 carbon pentose sugar and a nitrogenous base.

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3
Q

What nitrogenous bases are complementary in DNA

A

Adenine & Thymine

Cytosine and Guanine

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4
Q

What nitrogenous bases are complementary in RNA

A

Adenine binds with Uracil

Cytosine pairs with guanine

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5
Q

DNA codes for a certain type of protein to made through what processes

A

Transcription
Translation

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6
Q

Transcription

A

involves the copying of DNA stand into an mRNA strand

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7
Q

Translation

A

involves the reading mRNA strand to produce a polypeptide chain of amino acids in the ribosomes

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8
Q

Proteome

A

completeset of proteins in acell

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9
Q

Proteomics

A

the study of the structure and function of proteins as well as the way they function and interact with eachother.

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10
Q

Where is proteomics used

A

1.medical diagnosis
2. producing monoclonal antibodies to treat cancer and viruses
3. design drugs to produce various conditions

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11
Q

how proteins are so diverse/the differnet proteins

A
  1. Transport proteins

2.Receptors on the plasma membrane

  1. enzymes as biological catalyst that speed up chemical reactions
  2. antibodies
  3. hormones

6.structural proteins like hair and nails

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12
Q

Transport proteins

A

proteins that move ions and large molcules across the plasma membrane during facicilated diffusion

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13
Q

Receptors

A

receptors are proteins that bind to specific signalling molecules, initiating a celluar response and involved in signla transudction

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14
Q

signal transduction

A

the process of celluar communcation and response to external signals.

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15
Q

enzymes

A

biological catalayst that speeds up chemcial reactions

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16
Q

antibodies

A

proteins produce by the immune system to defend against foreign pathogens

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17
Q

Hormones

A

released by the endocrine gland to signal between different cells, or cause stimulation or inhibition

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18
Q

Chemical structure of AMINO ACIDS

A

carboxyl group(COOH)
Amino group(NH2)
R group(which determine the type of amino acid )
central carbon

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19
Q

How many amino acidsare there and of them how many are actually essientla

A

20 amino acids

9 are essiental amino acids because they are not produced in the body.

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20
Q

What are amino acids made of

A

C-carbon
H-hydrogen
O-oxygen
N-nitrogen
S-sulfur

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21
Q

R group

A

a group that contains a carbon andhydrogen attom attached to a moleucle and determines the type of amino acid

22
Q

what forms the primary structure of a protein

A

polypeptide chain

23
Q

Condensation polymerisation reaction

A

a chemical process where smaller molecules combine to form larger molecules, releasing a smaller molecule such as water in the process.

24
Q

What are the 4 levels of protein stuctures

A
  1. primary
    2.secondary
    3.tertiary
  2. quaternary
25
Q

What is a primary structure and when is it formed

A

a polypeptide chain of amino acids help together via peptide bonds

Primary structures is formed when amino acids are joined together through a condensation reaction and produced in SOME ribosomes through translation.

26
Q

Secondayr structure

A

formed when a polypeptide chain folds and coils forming hydrogen bonds between amino acids which forms an alpha helices and beta pleated sheet

27
Q

Tertiary structure

A

, refers to the 3D shape of a protein and is formed when secondary structures further fold by forming interactions and bonds between amino acids and the R group.Functions to determine the proteins shape and functiinalcapabitlies

28
Q

Types of interactions of the tertiary structures

A

disulfide bond(strong)

weak hydrogen or ionic bonds

hydrophobic interactions

29
Q

Quaternary structure

A

is formed when two or more polypeptide chains with tertiary structures join together.

functions to enhance proteins functionla capabilties

and not all proteins will have quantatary structures

30
Q

what are possible Changes to protein structures

A
  1. proteins can folded, based on the sequence of the amino acids in a primary structure is dependen
  2. one chnage in an amino acid will form a different protein OR the amino acid may no longer be functional due to that change
  3. Proteins can bestructure via denaturation when exposed to high temperatures or extreme PH levels
31
Q

Unfolding of protein structures results in

A

a loss of function and is irreversible

32
Q

what is a hormone and examples

A

released by the endocrine gland to signal between different cells, or cause stimulation or inhibition

Insulin is a hormone that maintains glucose levels by allowing glucose to enter the cell

33
Q

what the elements make up the proteins of the amino acid

A

CHON=
carbon, hydrogen, oxygen and nitrogen

34
Q

why are essiental amino acids knwon as essiental amino acids

A

they are known as essential amino acids because their not sythensised by the body, and therefore it is essential for these amino acids to consumed through ones diet.

35
Q

what is the signifance of an R group- 2 marks

A

R group provides the amino acid with its own identity

and the R group provides the amino acid its own chemical properties which determines how the amino acid will react with the eachother and the surrounding environments, and therefore this will determine their specific function.

36
Q

proteins have R groups that can be hydrophilic or hydrophobic.

eg Alenine is an amino acidwith a hydrophbic R group, whilst tryosine has an hydrophilic R group

which is more advantageous

A

tyrosine which has an hydrophilic R group is more advantageous because it can travel through the body to carry out bodily processes as 60% of the body is composed of water n it repels water.

37
Q

what happens to an hydrophobic R group of amino acid in the body.

A

hydrophobic molecules of the R group are carried by lipophobic or hydrophilic molecules through the bloodstream

38
Q

hydrogen can only bond with…. nitrogen can only bond with… oxygen cna only bondwith… and carbon can only bond with

A

hydrogen can only bond with one element at once

nitrogen can only bond with 3 elements at once

oxygen can only bond with 2 elements at once

carbon can only bond with 4 elements at one.

39
Q

beable to draw peptide bond

A
40
Q

when/how is a peptide bond formed

A

a peptide bond is formed between two amino acids.

41
Q

wehen the bonds between amiino acid is broken down the reaction is knwon as the

A

hydrolysis reaction

42
Q

how beta pleatedsheets and alpha sheets created

A

secondary structures LIKE alpha helicies and beata sheets are formed when the hydrogen of the amino group of one amino acid and the oxygen of the caboxyl group of another amino acid join together to create a hydrogen bond which is the flattened folding for beta sheets nad tight coils for alpha sheets.

43
Q

which sturcutres have functions and what arethose functions

A

Primary structures have NO FUNCTION

secondary structures have NO FUNCTION

tertiary structures have FUNCTIONwhich is to determinign the proteins shape and its functional capabilties.

quaternary have FUNCTION of enhancing the functional capabilties of the protein complex like enzyme catalasis

44
Q

a minium strucutre that a protein needs to be at to function

A

is the tertiary structure.

45
Q

examples of each type of structure

A

primary structure; peptide bonds

secondary: alpha helix and beat pleated sheets

tertiary: hydrogen bonds between the R groups, ionic bonds, ionic bonds, disulfide bridges, and hydrophobic interactions

quanternarystructure;haemoglobin

46
Q

an example of a quaternary structure

A

an example of quaternary is hemoglobin which contains 4 polypeptide chains and contains a prosthetic group of haem which contains an iron ion –> function: carry O2

47
Q

must be able to label structure of cell and organelles function

A
48
Q

what is the folding of a protein dependent on

A

the folding of the proteins is dependent on the sequence of amino acids in a primary structure

49
Q

when are proteins denatured

A

high temperatures or extreme high or low PH levels

50
Q

hydrolysis reaction

A

wehen the bonds between amiino acid is broken down the reaction

51
Q

function of RNA vs DNA

A

The function of DNA is to store genetic information for the long term, whilst the function of RNA is to to transfer genetic information.

Chapter 2- nucleic acids and proteins (6 decks)

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