biolab midterms Flashcards

1
Q

CH(NH2)COOH

A

Protein that consists of amino acids

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2
Q

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

A

Amino acids

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3
Q

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

A

Amino acids

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4
Q

compound consisting 2 or more amino acids.

A

Peptide

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5
Q

have 10 or fewer amino acids.

A

Oligopeptides

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6
Q

Peptides consisting more than 50 amino acids

A

Proteins

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7
Q

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

A

Biuret Test

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8
Q

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

A

blue violet color.

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9
Q

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

A

Cu2+ (Copper Iron)

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10
Q

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

A

65% Nitric Acid

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11
Q

Nitro derivates show intensely (?)

A

yellow color.

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12
Q

Biochemical test for the detection of amino acids containing aromatics

A

Xanthoproteic test

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13
Q

Used to detect presence of soluble proteins

A

Millon’s Test

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14
Q

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

A

Millon’s Test

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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)

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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

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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

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18
Q

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

A

purple-blue

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19
Q

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

A

Denaturation of Protein

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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.

24
Q

Gets disrupted by the addition of alcohol.

A

Hydrogen Bonding

25
- Used as a disinfectant for the skin
70% Alcohol
26
- Concentration of alcohol is able to penetrate the bacterial cell wall and denature the proteins and enzymes inside the cell wall.
70% Alcohol
27
- Merely coagulates the protein on the outside of the cell wall
95% Alcohol
28
- Prevents alcohol from entering the cell
95% Alcohol
29
(?) can be used to disrupt hydrogen bonds and non-polar hydrophobic interactions. increases kinetic energy and cause molecules to vibrate rapidly causing bond disruption.
Heat
30
Heat can be used to disrupt (?). - Heat increases kinetic energy and cause molecules to vibrate rapidly causing bond disruption.
hydrogen bonds and non-polar hydrophobic interactions
31
Heat increases (?) and cause molecules to vibrate rapidly causing bond disruption.
kinetic energy
32
● Tannate and Trichloroacetate are high molecular weight anions ● Negative charge of anions counteracts Positive charge of amino group in proteins, giving precipitate.
Alkaloidal Reagents
33
(?) are high molecular weight anions
Tannate and Trichloroacetate
34
Negative charge of anions counteracts Positive charge of amino group in proteins, giving (?)
giving precipitate.
35
● Disrupt salt bridges
Inorganic Acids
36
● Result from the neutralization of an acid and amine on side chains.
Salt Bridges
37
- ionic between positive ammonium group - ionic between negative acid group
Positive interaction
38
(?) disrupt salt bridges held together by ionic charges.
Inorganic acids
39
Inorganic acids disrupt salt bridges held together by (?)
ionic charges.
40
● Occurs when positive and negative ions in the salt change partners with the positive and negative ions in the new acid.
Double Replacement Reaction
41
● Occurs in the digestive system, where acidic gastric juices cause the coagulation of milk
Double Replacement Reaction
42
● 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.
Paper Chromatography
43
- Depends on properties such as molecular weight, structure, shape, and polarity of the molecule
The relative affinity
44
Higher affinity for mobile phase than stationary phase - Travels with solvent - Unimpeded by filter paper
Amino Acid Affinity
45
- Tends to stick to paper - Travels more slowly than the solvent front.
Higher affinity for paper than the solvent
46
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.
amino acid
47
Ninhydrin reacts with amino acids to form a (?)
blue-violet compound
48
The (?) defines the ratio of the distance moved by a particular component divided by the distance moved by the solvent
Rf value
49
(?) and (?) give positive result to the sulfur test
cysteine and cystine