Organic 25: Amino Acids, Peptides, & Proteins Flashcards

(32 cards)

1
Q

Amino acids

A

carboxylic acids that contain an amine function

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

Peptide bond

A

an amide bond between the carboxylic acid function of 1 amino acid and the amino nitrogen of another forms this type of bond

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

Dipeptide

A

molecule consisting of 2 amino acids joined by a peptide bond

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

Tripeptide

A

molecule consisting of 3 amino acids joined by 2 peptide bonds

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

Tetrapeptide

A

molecule consisting of 4 amino acids joined by 3 peptide bonds

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

Polypeptides

A

peptides with more then 30-50 amino acids

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

Proteins

A

polypeptides that have some biological function

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

Standard amino acids

A

group of 20 amino acids coded for in DNA-directed protein synthesis; all are alpha-amino acids; all but one contain a primary amino function

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

Essential amino acids

A

amino acids that must be obtained from one’s diet

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

Amino Acid Racemization (AAR)

A

novel technique for dating archaeological samples; based on the stereochemistry of amino acids

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

Zwitterion

A

the form in which neutral amino acids actually exist; the amino group is in its protonated form and the carboxyl group is present as a carboxylate

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

Isoelectric (isoionic) point

A

pH at which the amino acid has no net charge

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

N (amino) terminus

A

the left end of the peptide, contains the amino group

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

C (carboxyl) terminus

A

the right end of the peptide, containing the carboxyl group

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

Amino acid residues

A

individual amino acid components of peptides

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

Primary structure

A

amino acid sequence plus any disulfide links

17
Q

Peptidases

A

the enzymes that catalyze the hydrolysis of peptide bonds

18
Q

Peptide map

A

the collection of sequenced fragments of amino acids for a particular substance

19
Q

Edman Degradation

A

method for determining the N-terminal amino acid of a peptide or protein; involves treating the material with phenyl isothiocyanate (C6H5N=C=S), cleaving with acid, then identifying the phenylthiohydantoin (PTH derivative) produced

20
Q

Secondary structure

A

conformational relationship of nearest neighbor amino acids with respect to each other

21
Q

Alpha helix, Beta sheet

A

secondary structures of proteins

22
Q

Random coils

A

a portion of a protein that lacks an ordered secondary structure

23
Q

Tertiary structure

A

the way a protein chain is folded; affects both its physical properties and its biological function

24
Q

Fibrous

A

protein bundles of elongated filaments of protein chains; insoluble in water

25
Globular
spherical proteins; either soluble or form colloidal dispersions in water
26
Hydrophobic effect
the excluding of nonpolar molecules from water
27
Enzyme
a protein that catalyzes a chemical reaction in a living system
28
Active site
region of an enzyme at which a substrate is bound
29
Cofactors
a molecule that acts in combination with an enzyme to bring about a reaction; may either be a coenzyme or a prosthetic group
30
Coenzyme
cofactors that are organic molecules and not covalently bonded to the enzyme
31
Prosthetic group
cofactors that are organic molecules and ARE covalently bonded to the enzyme
32
Quaternary structure
description of the way in which 2 or more protein chains, not connected by chemical bonds, are organized in a larger protein