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Biology > 2.4 > Flashcards

2.4 Flashcards

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1
Q

what are proteins also known as

A

polypeptides

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2
Q

what is the basic unit of a polypeptide

A

amino acid - a carbon based compound with a carboxyl group (-COOH_ and an amino group (-NH2)

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3
Q

draw an amino acid

A

look online

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4
Q

draw a triglyceride

A

look online

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5
Q

draw a alpha d and beta d glucose molecule

A

look online

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6
Q

draw ribose

A

look online

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7
Q

draw a fatty acid

A

look online

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8
Q

draw a condensation reaction of two amino acids

A

look online

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9
Q

draw a condensation reaction of two alpha d glucose molecules

A

look online

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10
Q

what provides the water in the condensation of amino acids

A

the carboxyl provides OH

and the amino group provides H

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11
Q

what does the condensation of two amino acids produce and what bond

A

a dipeptide and a peptide bond

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12
Q

what are peptides

A

smaller than proteins, consists between 2 and 50 amino acids

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13
Q

what are proteins

A

polymers that are made up of 51 or more amino acids

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14
Q

how may different amino acids are found in proteins

A

20

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15
Q

how many different types of polypeptides can be form

A

20^n where n is the number of amino acids per polypeptide

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16
Q

where does the synthesis of polypeptides take place

A

on ribosomes in a process called translation

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17
Q

what do genes code for

A

they code for one polypeptide, a sequence of amino acids linked together by peptide bonds

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18
Q

how is genetic material transcribed

A

into ribonucleic acid (RNA) called mRNA (messenger RNA). this then carries the instructions for the amino acid sequence to the ribosome

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19
Q

name an example of a protein that consists of more than one polypeptide chain

A

hemoglobin, consists of four polypeptide chains and a non-protein part known as a heme group

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20
Q

what do R groups affect

A

they determine the types of bonds and interactions with other molecules

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21
Q

what can a single change in the order of amino acids cause

A

changes to a proton’s confirmation, resulting in a change of shape or loss of function

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22
Q

what can cause changes to the order of amino acids

A

gene mutations

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23
Q

what happens in sickle cell anemia

A

the glutamic acid is substituted by valine, causing sever changes to the structure f the hemoglobin

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24
Q

what is the primary structure of a protein

A

the sequence of Amino acids in a protein which defines all aspects of the structure and function of. a protein

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25
Q

what is the secondary structure

A

involves the folding of the chains on themselves to form pleated sheets or alpha helixes

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26
Q

what is the tertiary structure

A

when the polypeptide folds and coils to form a complex three dimensional shape

27
Q

what is the quaternary structure

A

only occurs in proteins that are mad up of two or more polypeptide chains and refers to the way the multiple subunits are held together in a multi-subunit complex.

28
Q

examples of proteins with quaternary structure

A

hemoglobin and rubisco

29
Q

what is hemoglobin made of

A

quaternary structure - has two alpha and two beta chains, together with the heme group, it forms a functional structure that can transport four molecules of oxygen

30
Q

What would happen if a single amino acid in a protein consisting of 325 amino acids were changed?

A

the primary structure as well as the tertiary suture would be altered

31
Q

example of a tertiary structure

A

lysosomes - 3dimensional shape

32
Q

what si a genome

A

the complete and unique set of DNA

33
Q

what does the genome code for

A

Proteins

34
Q

what is a proteome

A

a unique set of proteins

35
Q

what is proteome analysis

A

a new tool in medical research and cancer treatment

36
Q

why is gel electrophoresis used

A

to separate proteins and allays a proteome of a species

37
Q

what are the two types of proteins based on their solubility in water

A

globular and fibrous proteins

38
Q

example of a fibrous protein

A

collagen

39
Q

example of a globular protein

A

hemoglobin

40
Q

what are global proteins

A

usually soluble in water because their hydrophobic R group is folded into the core of the molecule

globe like or spherical

play active roles in the cells metabolism

consist of complex polypeptide chains

41
Q

what are fibrous proteins

A

fibre long and thread like

usually made of long polypeptide chains where the hydrophobic R groups are exposed making the molecule insoluble

they are often found in structural parts of organisms such as tendons and skin

42
Q

usual roles of globular proteins

A

active role in cells membrane

43
Q

role of fibrous proteins

A

structural parts of organisms such as tendons and skin

44
Q

Examples of globular proteins

A

rubisco
insulin
immunoglobulin
rhodopsin

45
Q

examples of fibrous proteins

A

collagen and spider silk

46
Q

function of rubisco

A

an enzyme involved in the fixation of CO2 in chloroplasts

47
Q

role of insulin

A

a hormone produced by the beta cells of the pancreas which is involved in glucose uptake from the blood

48
Q

role of immunoglobulin

A

large Y shaped proteins called antibodies

involved in fighting infections by specifically recognizing and binding to antigen molecules

49
Q

role of rhodopsin

A

a protein linked to pigment found on the membrane of rod (photoreceptor) cells of the retina where it allows very low light intensities to be detected

50
Q

role of collagen

A

structural protein found in muscles tendons and ligament, where it gives tensile strength and occurs in skin and bones where it prevents tearing and fractures respectively

51
Q

role of spider silk

A

a fibrous protein produced by spiders for their webs can be extended and very resistant to breaking

52
Q

what is denaturation

A

a process in which proteins lose their secondary and tertiary structures

53
Q

what happens when amino acids are disrupted

A

active sites lose their shape, the whole enzyme loses its enzymatic properties

54
Q

what are two ways of denaturing proteins

A

high temps and changing pH

55
Q

how does temperature cause denaturation

A

when there are very high temperatures, proteins denature and loose their confirmation as the interaction between certain amino acids change, quaternary and tertiary structures and in extreme conditions, the secondary structures are irreversibly changes.

this results in loss of forma and function

however, peptide bonds do not break during the denaturation process, therefore, the primary structure of the protein is not disrupted

56
Q

what is not disrupted in denaturation by temperature

A

the primary structure

57
Q

how does PH cause denaturation

A

strong alkaline or acidic solutions can break the bonds between the non-adjacent amino acids or between the polypeptide chains of quaternary proteins resulting in denaturation and loss of functionality

58
Q

how are integral globular proteins formed

A

globular membrane proteins have hydrophobic r groups on the outside of the protein

globular water soluble proteins have hydrophilic r groups on the outside of the cell

59
Q

what protein is made up of three different polypeptide chains

A

collagen

60
Q

What is the fundamental chemical group that varies among various types of amino acids?

A

R groups

61
Q

What is an enzyme involved in the fixation of CO2 in chloroplasts?

A

Rubisco

62
Q

what is the basic unit of a polypeptide made up of

A

carbon based compound containing nitrogen and hydrogen

63
Q

hydrophobic R groups of globular proteins are usually …

A

folded into the protein core, since most globular proteins are water soluble

Biology (51 decks)

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