Carbohydrate Metabolism Basics Flashcards

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1
Q

A monosaccharide is

& its molecular formula is

A

a single carbohydrate molecule also known as a simple sugar’

CnH2nOn

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2
Q

Two monosaccharides bonded together is

A

A disaccharide

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3
Q

A few monosaccharides bonded together is

A

A oligosaccharide

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4
Q

Many monosaccharides bonded together is

A

polysaccharide

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5
Q

The bond between two simple sugars is referred to as

A

a glycosidic linkage

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6
Q

Glycosidic linkage bond is formed how?

A

Through a dehydration reaction that require enzymatic catalysis

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7
Q

Sucrose is made up of which two monosaccharides?

A

glucose and fructose

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8
Q

Lactose is made up of which two monosaccharides?

A

galactose and glucose

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9
Q

How are monosaccharides created in order to be used in metabolic pathways (thus be used for energy)?

A

Through hydrolysis of polysaccharides - enzymatic catalysis is necessary to move reaction forward but still favored thermodynamically

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10
Q

In cellular respiration, the high-energy electron carriers are?

A

NAD+ and FAD (NADH and FADH2 before oxidation)

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11
Q

NADH and FADH2 both serve as

A

enzymatic cofactors

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12
Q

The four step process of glucose being oxidized to produce CO2 and ATP is

A

glycolysis, pyruvate dehydrogenase complex (PDC), Krebs cycle, and electron transport/oxidative phosphorylation

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13
Q

primary protein structure refers to the

A

amino acid sequence that makes up a protein

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14
Q

secondary protein structure refers to the

A

arrangement in space of the peptide backbone of a protein

*only two bonds have free rotation

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15
Q

in secondary protein structure, alpha-helix are

A

side chains that radiate out from the helix axis

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16
Q

in secondary protein structure, the alpha-helix contain hydrogen bonds that are

A

parallel to the helix axis

17
Q

in secondary protein structure, the alpha-helix coil is what direction

A

clockwise (right-handed)

18
Q

in secondary protein structure, beta-sheet are

A

side chains that alternate forces of the sheet

19
Q

in secondary protein structure, beta-sheet strands orientation are

A

parallel (polypeptide stands run in same direction) or anitparallel (polypeptide stands run in opposite direction)

20
Q

in secondary protein structure, beta-sheet is stabilized by

A

hydrogen bonding between the NH and CO groups in backbone

21
Q

tertiary protein structure refers to

A

the interactions of side chains
hydrophobic/hydrophilic interactions
covalent/non covalent interactions
electrostatic interactions

22
Q

tertiary protein structure, van der Waals forces occurs between

A

nonpolar side chains

23
Q

tertiary protein structure, hydrogen bonding occurs between

A

polar side chains (Ser, Thr)

24
Q

tertiary protein structure, disulfide bonds occur between

A

cysteine residues

25
Q

tertiary protein structure, electrostatic interactions occur between

A

amino acids with opposite charge thus acidic and basic side chains thus attraction
amino acids with like charge thus repulsion

26
Q

quaternary protein structure refers to

A

interactions between polypeptide subunits

dimers, trimers, tetramers

27
Q

quaternary protein structure have noncovalent interactions such as

A

electrostatic, hydrogen bonds, and hydrophobic interactions