structure and function of proteins Flashcards

1
Q

primary structure

A

sequence of amino acid residues

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

secondary

A

the localised conformation of the polypeptide backbone

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

tertiary

A

the three-dimensional structure of an entire polypeptide, including all its side chains

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

quaternanry

A

the spatial arrangement of polypeptide chains in a protein with multiple subunits

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

types of secondaery structures

A

alpha helix
beta strands and sheets
triple helix

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

bonds in the polypeptide backbone

A

hydrogen

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

alpha helix

A

rod like
one poly p chain

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

are beta sheets parallel or antiparallel

A

both

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

what is the most abundant protein in vertebrates

A

collagen triple helix

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

collagen triple helix

A

component of bone and connective tissue

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

what proteins are in tertiary structures

A

fibrous and globular

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

fibrous proteins

A

Contain polypeptide chains organized approximately parallel along a single axis. They
consist of long fibers or large sheets
tend to be mechanically strong
are insoluble in water and dilute salt solutions
play important structural roles in nature

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

examples of fibrous

A

keratin of hair and wool

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

examples of globular

A

myo and haemoglobin

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

globular protiens

A

Proteins which are folded to a more or less spherical shape
they tend to be soluble in water and salt solutions
most of their polar side chains are on the outside and interact with the aqueous environment by hydrogen bonding and ion-dipole interactions
most of their nonpolar side chains are buried inside
nearly all have substantial sections of alpha-helix and beta-sheet

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

forces stabilising tertiary structures

A

covalent disulphide bonds
Hydrophobic interactions
Hydrogen bonds
ionic bonding

17
Q

haemoglobin componentns

A

each subunit can bind one oxygen molecule
four subunits
two  and two  chains-beta and alpha
each contains a haem group

18
Q

can the body make essential amino acids

A

no they must come from foods