Brainscape's Knowledge GenomeTM

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


See full index

Bio chem > Lecture 4 - Building Blocks of Proteins > Flashcards

Lecture 4 - Building Blocks of Proteins Flashcards

1
Q

Zwitterion

A

Both positive and negative charges

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

Non polar

A

hydrophobic

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

Amino acids have

incl hows its classed

A

ionisable groups

Classed using pKa

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

pKa

A

pH where an ionisable group is half ionized

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

pI

isoelectric point

A

pH where the whole molecule has a charge of 0

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

Amino acid properties

A 
Amino Group (NH2)
Carboxyl Group (COOH)
Sidechain (R)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Amino acid are

A

Chiral

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

What do 20 amino acids have?

A 
Same backbone
Different sidechains (R)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Each amino acid has a different

A

name

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

Sidechains of amino acids in proteins are arranged to

A

carry out chemical reactions

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

Amino acid sidechain perform

A

biochem of proteins

attach to protein backbone

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

Non polar amino acids

A 
Glycine
Alanine
Valine
Leucine
Isoleucine
Methionine
F (Phenylalanine)
W (Tryptophan)
Cysteine
Proline

“Grandma Always Visits London In May For Winston’s Christmas Party”

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

Negatively charged (acidic) polar amino acids

A 
Aspartic acid (D)
Glutamic acid (E)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Positively charged (basic) polar amino acids

A

K (Lysine)
R (Arginine)
Histidine

“Knights Riding Horses”

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

Uncharged polar amino acids

A 
Threonine (Thr)
Q (Glutamine, Gln)
Serine
Y (Tyrosine, Tyr)
N (Asparagine, Asn)

“The Queen Stole Your Nose”

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

Why are 1 letter abbreviations for amino acids useful?

A

Sequence alignment

Describe mutations

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

Why are 1 letter abbreviations for amino acids useful example
Old way
“From a glutamate to a valine at position 6”
whats the new way

A

E6V

1st letter - wild type or native amino acid
Number - Location of mutation
2nd letter - Mutated residue

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

Some amino acids have

A

ionisable groups

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

what parts of amino acids in solution are usually charged?

A

amino and carboxyl ends

20
Q

Some amino acid side chains are

Incl which contribute to?

A

ionisable

net charge of the amino acid

21
Q

How can ionisable side chains of amino acids be classified?

A

pKa value

22
Q

Amino acids ionisable side chains examples

A 
Aspartic acid
Glutamic acid
Histidine
Lysine
Arginine
Cysteine
Tyrosine
23
Q

pKa value for an ionizable group on an amino acid or

protein is

A

pH at which the group is 50% ionized

24
Q

pI, or isoelectric point is

A

pH at which the net

charge on an amino acid (or protein) is zero

25
Q

all amino acids start out as

A

standard 20

26
Q

standard 20 of amino acids are

A

“translated” from RNA into proteins at the ribosome

27
Q

“post-translational modification”

A

amino acids modified after they are added to a

protein

28
Q

“post-translational modification” example

A

disulfide bond between 2 cysteines

29
Q

Other Amino Acid Modifications

A
  1. Phosphorylation (add phosphate)
  2. Hydroxylation (add hydroxyl)
  3. Carboxylation (add carboxyl)
  4. Metal Binding (add metal)
  5. Iodination (add iodine)
  6. Glycosylation (add glucose)
30
Q

Phosphorylation

A

control enzyme activity –

ON/OFF

31
Q

Hydroxylation

A

prevent connective tissues diseases and scurvy

32
Q

Carboxylation

A

need for blood clotting

metal binding

33
Q

Examples of Some Amino Acids that can be modified after translation

A

Phosphoserine
Phosphothreonine
Phosphotyrosine

Glycosylation of Threonine

34
Q

How are proteins made?

A

joining amino acids together with a covalent peptide bond

35
Q

Peptide

A

short stretch of amino acids joined together by peptide bonds

36
Q

Protein

A

long chain of amino acids joined together with a biological function

37
Q

amino acid residues

A

amino acids bond together

no longer complete, individual, amino acids.

38
Q

How did Linus Pauling and Robert Corey determine structure of peptide bond?

A

X ray Crystallography

39
Q

The Peptide Bond

A

Planar
Trans
Dipole

40
Q

What do we mean by “amino acids are chiral”?

A

exist in two forms have D- and L-isomers of amino acids.

have at least one chiral centre.

central carbon has four different groups attached

41
Q

What are the 4 main groups of amino acids, as discussed in the lecture?

A

Non Polar
-‘ve Polar (acid)
+‘ve Polar (basic)
Uncharge Polar

42
Q

Where in a protein would you expect to find non-polar amino acid residues?

A

Interior
hydrophobic
away from water

43
Q

What chemical groups would we expect to find in the R-group of an ionizable amino acid?

A 
Aspartic Acid (pKa = 4)
Glutamic Acid (4)

Histidine (6)
Lysine (10)
Arginine (12.5)

Cysteine (8)
Tyrosine (10)

44
Q

What is the name of the bond that links amino acids in the polypeptide chain?

A

Peptide bond (Covalent bond)

45
Q

What are the key properties of peptide bond?

A

Planar, trans, dipole

46
Q

List some common examples of post-translational modifications.

A
  1. Phosphorylation (add phosphate)
  2. Hydroxylation (add hydroxyl)
  3. Carboxylation (add carboxyl)
  4. Metal Binding (add metal)
  5. Iodination (add iodine)
  6. Glycosylation (add glucose)
47
Q

What are some important functions of posttranslational modifications?

A

control enzyme activity –
ON/OFF

prevent connective tissues diseases and scurvy

need for blood clotting
metal binding

Bio chem (36 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions