Brainscape's Knowledge GenomeTM

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


See full index

TFN > biolab midterms > Flashcards

biolab midterms Flashcards

1
Q

CH(NH2)COOH

A

Protein that consists of amino acids

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

(?) link to each other when the carboxyl group of one molecule reacts with the amino group of another molecule.

A

Amino acids

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

Basic building blocks of enzymes, hormones, proteins, and body tissues.

A

Amino acids

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

compound consisting 2 or more amino acids.

A

Peptide

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

have 10 or fewer amino acids.

A

Oligopeptides

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

Peptides consisting more than 50 amino acids

A

Proteins

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

Used for quantitative photometrical determination of total protein concentration. (Intensity of color that is produced)

A

Biuret Test

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

Peptides and protein react with Cu2+ (Copper Iron) in alkalinity to create a (?)

A

blue violet color.

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

Peptides and protein react with (?) in alkalinity to create a blue violet color.

A

Cu2+ (Copper Iron)

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

Using (?) the aromatic rings of amino acids like tyrosine and tryptophan are nitrated.

A

65% Nitric Acid

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

Nitro derivates show intensely (?)

A

yellow color.

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

Biochemical test for the detection of amino acids containing aromatics

A

Xanthoproteic test

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

Used to detect presence of soluble proteins

A

Millon’s Test

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

Reddish-brown coloration or precipitate indicates the presence of tyrosine residue (Occurs in nearly all proteins)

A

Millon’s Test

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

Sulfur-containing amino acids when boiled converts into an inorganic sulfide (Na2S, Sodium Sulfide) - Reacts with lead acetate to form a (?) - Cysteine and Cystine give positive result to the sulfur test.

A

black precipitate of PbS (Phosphate-Buffered Saline)

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

(?) containing amino acids when boiled converts into an inorganic sulfide (Na2S, Sodium Sulfide) - Reacts with lead acetate to form a black precipitate of PbS (Phosphate-Buffered Saline) - Cysteine and Cystine give positive result to the sulfur test.

A

Sulfur

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

● Test for indole ring of tryptophan condensed with glyoxylic acid in the presence of sulfuric acid ● Forms violet-colored complex

A

Hopkins-Cole Test

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

When it reacts with Ninhydrin, a (?) complex is formed.
Test is given by ALL proteins

A

purple-blue

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

disruption and possible destruction of both the secondary and tertiary structure.

A

Denaturation of Protein

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

The (?) remains the same after the denaturation process.

A

primary structure

21
Q

Occurs between amide groups in the secondary protein structure

A

Hydrogen Bonding

22
Q

occurs in tertiary protein structures - In a variety of amino acid combinations

A

Hydrogen Bonding

23
Q

(?) denatures proteins by disrupting the side chain intramolecular hydrogen bonding.

A

Alcohol

24
Q

Gets disrupted by the addition of alcohol.

A

Hydrogen Bonding

25
Q
  • Used as a disinfectant for the skin
A

70% Alcohol

26
Q
  • Concentration of alcohol is able to penetrate the bacterial cell wall and denature the proteins and enzymes inside the cell wall.
A

70% Alcohol

27
Q
  • Merely coagulates the protein on the outside of the cell wall
A

95% Alcohol

28
Q
  • Prevents alcohol from entering the cell
A

95% Alcohol

29
Q

(?) can be used to disrupt hydrogen bonds and non-polar hydrophobic interactions. increases kinetic energy and cause molecules to vibrate rapidly causing bond disruption.

A

Heat

30
Q

Heat can be used to disrupt (?). - Heat increases kinetic energy and cause molecules to vibrate rapidly causing bond disruption.

A

hydrogen bonds and non-polar hydrophobic interactions

31
Q

Heat increases (?) and cause molecules to vibrate rapidly causing bond disruption.

A

kinetic energy

32
Q

● Tannate and Trichloroacetate are high molecular weight anions
● Negative charge of anions counteracts Positive charge of amino group in proteins, giving precipitate.

A

Alkaloidal Reagents

33
Q

(?) are high molecular weight anions

A

Tannate and Trichloroacetate

34
Q

Negative charge of anions counteracts Positive charge of amino group in proteins,
giving (?)

A

giving precipitate.

35
Q

● Disrupt salt bridges

A

Inorganic Acids

36
Q

● Result from the neutralization of an acid and amine on side chains.

A

Salt Bridges

37
Q
  • ionic between positive ammonium group
  • ionic between negative acid group
A

Positive interaction

38
Q

(?) disrupt salt bridges held together by ionic charges.

A

Inorganic acids

39
Q

Inorganic acids disrupt salt bridges held together by (?)

A

ionic charges.

40
Q

● Occurs when positive and negative ions in the salt change partners with the positive and negative ions in the new acid.

A

Double Replacement Reaction

41
Q

● Occurs in the digestive system, where acidic gastric juices cause the coagulation of milk

A

Double Replacement Reaction

42
Q

● Distribution of the solute between a polar liquid phase
● Strongly absorbed on the cellulose fibers of paper
● Moves up the paper, amino acid is carried to a particular position on paper.

A

Paper Chromatography

43
Q
  • Depends on properties such as molecular weight, structure, shape, and polarity of the molecule
A

The relative affinity

44
Q

Higher affinity for mobile phase than stationary phase
- Travels with solvent - Unimpeded by filter paper

A

Amino Acid Affinity

45
Q
  • Tends to stick to paper
  • Travels more slowly than the solvent front.
A

Higher affinity for paper than the solvent

46
Q

An (?) that is highly soluble in the eluting solvent will have a higher affinity for the mobile phase than an amino acid that is less soluble in the solvent.

A

amino acid

47
Q

Ninhydrin reacts with amino acids to form a (?)

A

blue-violet compound

48
Q

The (?) defines the ratio of the distance moved by a particular component divided by the distance moved by the solvent

A

Rf value

49
Q

(?) and (?) give positive result to the sulfur test

A

cysteine and cystine

TFN (31 decks)

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