Peptides Flashcards

1
Q

A compound containing
two amino acids is specifically called a

A

dipeptide

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

is an unbranched
chain of amino acids, each joined to the next by a peptide bond

A

peptide

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

three amino acids joined together in
a chain constitute a

A

tripeptide

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

s loosely used to refer
to peptides with 10 to 20 amino acid residues

A

oligopeptide

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

is a long unbranched chain of amino acids, each
joined to the next by a peptide bond.

A

Polypeptide

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

is a covalent bond between the carboxyl group of one amino acid and the amino group of another amino acid.

A

Peptide bond

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

The end with the free H3N+ group is called

A

N terminal end

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

end with the free COO- group is called the

A

C terminal end

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

s the portion of an amino acid structure that remains, after the release of H2O, when an amino acid participates in peptide bond formation as it becomes part of a peptide chain

A

amino acid residue

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

The two best-known peptide hormones, both produced by the pituitary gland,

A

oxytocin
and vasopressin

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

are pentapeptide neurotransmitters produced by the brain itself that bind at
receptor sites in the brain to reduce pain

A

Enkephalins

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

Met-enkephalin

A

Tyr–Gly–Gly–Phe–Met

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

Leu-enkephalin

A

Tyr–Gly–Gly–Phe–Leu

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

is a protein in which
only one peptide chain is present

A

monomeric protein

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

is a protein in which more than one
peptide chain is present

A

multimeric protein

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

is a protein in which only amino acid residues are present

A

simple protein

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

The peptide chains present in multimeric proteins are called

A

protein subunits.

16
Q

is a protein that has one or more non amino acid entities present in its structure in addition to one or more peptide chains.

A

conjugated protein

17
Q
A
18
Q

is a non-amino acid group present in a conjugated protein.

A

prosthetic group

19
Q

contain carbohydrate groups

A

glycoproteins

20
Q

contain lipid prosthetic groups

A

Lipoproteins

21
Q

contain a specific metal, and so on.

A

metalloproteins

22
Q

These four protein structural levels, listed in order of increasing complexity, are?

A

Primary, secondary, tertiary, quaternary structure

23
Q

Who work the to determined the primary structure?

A

Frederick Sanger

24
Q

is the order in which amino acids are linked together in a
protein

A

Primary protein

25
Q

is the arrangement in space adopted by the backbone portion of a protein.

A

Secondary protein structure

26
Q

Give me The two most common types of secondary structure are..

A

Alpha Helix and Beta pleated sheet

27
Q

s a protein secondary structure in which a single protein
chain adopts a shape that resembles a coiled spring (helix), with the coil configuration maintained by hydrogen bonds

A

alpha helix structure

28
Q

is a protein secondary structure in which two fully extended protein chain segments in the same or different molecules are held together by hydrogen bonds

A

beta pleated sheet structure

29
Q

is the overall three-dimensional shape of a protein that
results from the interactions between amino acid side chains (R groups) that are widely separated from each other within a peptide chain

A

Tertiary protein structure

30
Q

Give me the Four types of attractive interactions contribute to the tertiary structure of a protein

A

Covalent Disulfide bonds, Electrostatic attractions, hydrogen bonds, hydrophobic attractions.

31
Q

is the organization among the various peptide chains in
a multimeric protein

A

Quaternary protein structure

32
Q

is a protein whose molecules have an elongated shape with one dimension much longer than the others

A

fibrous protein

33
Q

is a protein whose molecules have peptide chains
that are folded into spherical or globular shapes

A

A globular protein

34
Q

is a protein that is found associated with a membrane system of a cell

A

membrane protein

35
Q

this hemoglobin has a greater affinity for oxygen than the mother’s hemoglobin

A

fetal hemoglobin

36
Q
A
37
Q
A
38
Q
A