PUGAD BIOCHEM Flashcards

0
Q

Has a polar, uncharged R group

A

Cysteine

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1
Q

Has a nonpolar R group

A

Valine

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2
Q

Has a nonpolar R group

A

Alanine

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3
Q

Has a negatively charge R group

A

Aspartic acid / Aspartate

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4
Q

The naturally occurring tranquilizer of the body is derived from this amino acid

A

Glutamic acid

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5
Q

Is the form of a molecule that has an equal number of positive and negative charges and thus is electrically neutral

A

Isoelectric species

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6
Q

Is the amino acid arrangement maintained by peptide bonds

A

Primary level

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7
Q

Are maintained by hydrogen bonds between at groups and other special bonds such as the disulfide bridge between cysteine

A

Tertiary and quarternary level

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8
Q

Are the two most commonly seen secondary level structures.

A

Alpha helix and beta helix

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9
Q

The stability of it arises primarily from hydrogen bonds formed between the oxygen of the peptide bond carbonyl and the hydrogen atom of the peptide bond nitrogen of the fourth residue down the polypeptide chain

Sheets derive much of their stability from hydrogen bonds between the carbonyl oxygen and amide hydrogen of peptide bonds

A

Alpha helix

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10
Q

The most visible effect of denaturation on proteins

A

Decreased solubility

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11
Q

Separates compounds based on their chemical properties and by extension their solubility

A

Paper chromatography

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12
Q

Separates on the basis of size

A

Gel-infiltration chromatography

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13
Q

Separates on the basis of their net charge

A

Ion-exchange chromatography

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14
Q

Takes advantage of the high affinity of many proteins for specific chemical groups

A

Affinity chromatography

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15
Q

This could be a limiting amino acid in an incomplete protein

A

Tryptophan

16
Q

Oxidative deamination refers to the removal of an amine group.

A

Glutamate dehydrogenase

17
Q

Catalyzes the reaction of glutamate and NH4+ to glutamine in the mitochondria

A

Glutamine synthetase

18
Q

Catalyzes the reaction of glutamine to glutamate and NH4+

A

Glutaminase

19
Q

L-amino acid oxidase is a class of oxidoreductase that reacts an L-amino acid to its 2-oxo form and NH4+

A

L-amino acid oxidase

20
Q

Is found as a dimer in secretions mainly found on the surface of epithelial cells

21
Q

Is a B-cell receptor associated with normal B cell development

22
Q

Efficiently opsonizes pathogen for engulfment by phagocytes and activates the complement system

23
Q

The first antibody in development and response because it is produced before B cells have undergone somatic hypermutation

24
Is bound by receptors on mast cells, causing antigen binding to release powerful chemical mediators involved in allergic responses
IgE
25
Classical pathway of complement activation Is not specific to any one pathogen but rather constitutes a first line of defense
Innate immunity
26
This pathway can convert glucose to ascorbic acid Catalyzes the conversion of glucose to glucuronic acid to ascorbic acid
Glucuronic acid/uronic pathway
27
Also known as the glycolysis pathway
Embden-Meyerhof pathway
28
A process that generates NADPH and penthouses
Pentose phosphate pathway / phosphogluconate
29
Is also known as 1,25-dihydroxyvitamin D because it has two hydroxy groups on carbon 1 and 25 by the enzyme calciol-25-hydroxylase in the liver and calcidiol-1-hydroxylase in the kidney
Activated VITAMIN D
30
Induces squamous metaplasia in the respiratory epithelium
Deficiency of vitamin A (retinoic acid)
31
This is a test for folic acid deficiency
Histidine load test
32
This vitamin functions as coenzyme in the major anaplerotic reaction of the body Is a coenzyme active when covalently attached to a carboxylase, participating in carboxylation reactions
Biotin
33
Is the addition of a carboxylic acid group to a substrate such as in the formation of oxaloacetate by the carboxylation of pyruvate, catalyzed by pyruvate carboxylase
Carboxylation
34
Are those that form intermediates of metabolic pathway
Anaplerotic reactions
35
Has been shown to correlate the iron absorption
Vitamin B6 / Pyridoxine deficiency