Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

STRUC+FUNC 1 (vet) > Amino Acids and Proteins > Flashcards

Amino Acids and Proteins Flashcards

1
Q

how many amino acids are found in nature?

A

more than 700

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

how many AA are building blocks for proteins in cells?

A

22

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

structure of an amino acid?

A

amino group, carboxyl group, side chain (defines the chemical characteristics of the amino acid - variable R group)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

what can an amino acid be classified depending on?

A

the chemical characteristics of their side chains
synthesis
essential/non-essential

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

what are the possible chemical characteristics of the amino acids side chains?

A

polar
non-polar
charged
non-charged
aliphatic
aromatic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

types of synthesis of amino acids?

A

proteinogenic
non-proteinogenic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

types of ‘essential’ of an amino acid?

A

essential
conditionally essential
non-essential

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

what makes a side chain polar?

A

if it has an oxygen or nitrogen on the end of the side chain e.g. OH, NH2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

what makes a side chain non-polar?

A

if there is no polar molecule at the end of the side chain e.g. CH3

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

what charge does the amino acid have if the side chain is basic?

A

positive charge

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

what charge does the amino acid have if the side chain is acidic?

A

negative charge

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

proteinogenic amino acids?

A

they are the building blocks of proteins
20 are encoded by triplets of the genetic code

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

selenocysteine and pyrrolysine both contain a structural change in the mRNA sequence, what does this allow?

A

allows a STOP codon not to be recognised as such by a specific tRNA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

non-proteinogenic amino acids functions?

A

can have other biological functions beyond forming proteins
e.g. GABA (neurotransmitter)
Carnitine (transport of fatty acids in the blood)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

non-proteinogenic amino acid synthesis?

A

they are not produced directly and in isolation by standard cellular machinery

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

when and how are non-proteinogenic amino acids modified?

A

modified by post-translational modification of the protein in which they are embedded
occurs post-translationally, once the protein has already formed
often linked to the function/activity of the protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

what are the common modifications of non-proteinogenic amino acids?

A

phosphorylation
methylation
acetylation
hydroxylation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

give some example of essential amino acids?

A

His, Ile, Leu, Lys, Met, Phe, Thr, Trp and Val

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

give example of conditionally essential amino acids:

A

Arg, Cys, Gln, Tyr, Gly, Pro and Ser

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

what are essential amino acids?

A

the ones that can’t be synthesised by the body and must be obtained through the diet

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

what are conditionally essential amino acids?

A

in condition of stress, a surplus of these amino acids need to be uptaken through the diet to cope with body demand

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

give examples of non-essential amino acids:

A

Ala, Arg, Agn, Asp, Cys, Glu, Gln, Gly, Pro, Ser and Tyr

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

what are non-essential amino acids?

A

CAN be synthesised by the body

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

what does lignin do?

A

it reduces the absorption of nutrients

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

what do herbivores eat?

A

hay, straw, haylage

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

what does hay/straw/haylage have high levels of?

A

lignin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

hay/straw/haylage - decreased levels of?

A

essential AA such as Lys

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

functions of proteins?

A

storage, enzyme, transport, protection, hormonal, contractile, receptor, structural

29
Q

contractile protein example?

A

actin and myosin

30
Q

hormonal protein example?

A

insulin

31
Q

protection protein example?

A

immunoglobulin (antibody)

32
Q

transport protein example?

A

haemoglobin

33
Q

enzyme protein example?

A

Rubisco

34
Q

storage protein example?

A

ferritin

35
Q

structural protein example?

A

spider silk

36
Q

receptor protein example?

A

rhodopsin

37
Q

primary protein structure?

A

is a sequence of a chain of amino acids

38
Q

what are amino acids bound together through?

A

peptide (amide) bonds

39
Q

protein?

A

polypeptide chain

40
Q

dehydration synthesis reaction?

A

condensation reaction

41
Q

the alpha helix structure is not what?

A

it is not a hollow structure, it is just a very tight spiral

42
Q

what kind of spiral conformation is the alpha helix?

A

right hand spiral conformation

43
Q

what does every backbone NH donate?

A

donates a hydrogen bond to the backbone C=O group of the amino acid lovated 3-4 residues earlier along the protein sequence

44
Q

what does the Beta structure consist of?

A

Beta strands and Beta sheets

45
Q

What are Beta strands?

A

portions of the polypeptide chain that are almost fully extended having a ‘zig-zag’ shape

46
Q

Beta strands are flexible but not?

A

they are flexible but not elastic

47
Q

Where can the H bonded Beta strands be found?

A

on separate polypeptide chains or on different segments of the same chain

48
Q

how do the Beta strands in a sheet run?

A

can either be parallel (running in the same N- to C- terminal direction) or antiparallel (running in the opposite N- to C- terminal direction)

49
Q

what are Beta sheets?

A

when multiple Beta strands are arranged side-by-side they form Beta sheets

50
Q

What are beta sheets stabilised by?

A

by hydrogen bonds between between carbonyl oxygens and amide hydrogens on adjacent B strands

51
Q

why do proteins rarely contain isolated B strands?

A

because the structure by itself is not significantly more stable than other conformations

52
Q

what weak bonds stabilise the proteins tertiary structure?

A

hydrogen bonds
electrostatic interactions
hydrophobic interactions

53
Q

where are cysteine bonds found between?

A

between cysteines

54
Q

two major classes of proteins tertiary structure?

A

fibrous and globular

55
Q

amphipathic?

A

both hydrophilic and hydrophobic parts to the molecule

56
Q

tertiary protein structure?

A

occurs when certain attractions/interactions are present between alpha helixes and pleated sheets

57
Q

secondary protein structure?

A

occurs when the sequence of amino acids are linked by hydrogen bonds

58
Q

primary protein structure?

A

a sequence of a chain of amino acids

59
Q

quaternary protein structure?

A

is a protein consisting of more than one amino acid chain

60
Q

give examples of hydrophobic amino acids:

A

leucine and isoleucine

61
Q

give examples of hydrophilic amino acids:

A

serine or threonine

62
Q

alpha anylase?

A

begins breakdown of carbs in our saliva

63
Q

what leads to misfolded proteins?

A

mutation in their amino acid sequence
error in the folding process

64
Q

harmful effects of protein misfolding?

A

loss of function e.g. cystic fibrosis
gain of function e.g. alzheimer, parkinson, huntington’s (amyloid structure formation)

65
Q

sickle-cell anaemia?

A

mutation in haemoglobin

66
Q

what happens to untreated mutated (for sickle cell) homozygous?

A

generally die in childhood

67
Q

heterozygous individuals for sickle cell often show?

A

resistance to malaria

68
Q

how does the mutation result in sickle cell anaemia?

A

glu6>Val in the side chain of Hb so the new valine side chain can bind to a diffetent Hb molecule to form a strand which sickles the red blood cells

69
Q
A

STRUC+FUNC 1 (vet) (24 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions