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nbde biochem > 260-269 > Flashcards

260-269 Flashcards

1
Q

https://drive.google.com/open?id=0B8uJUY-tie8GZkctcXdsVUZPZUE

A

https://drive.google.com/open?id=0B8uJUY-tie8GSkpXS2ZJc1hfNnc

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2
Q

insulin

A

A homopolymer of fructose.

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3
Q

insulin

A

Highly water soluble.

■ Used to determine glomerular filtration rate (GFR).

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4
Q

Heteropolymer chains containing repeating disaccharide units of an amino

sugar (N-acetylglucosamine, N-acetylgalactosamine) and a uronic acid

(glucaronic acid, iduronic acid).

A

GLYCOSAMINOGLYCANS (GAGS )

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5
Q

The major structural polysaccharides of extracellular matrix (ECM), connective

tissue (CT), and outer cell membrane surfaces.

A

GAG

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6
Q

GAG

A

Because they contain sulfate and carboxyl groups, GAGs are highly negatively

charged and easily attract water, enabling them to cushion their surrounding

structures.

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7
Q

Accumulation of various GAGs (due to enzyme deficiencies) results in

several syndromic diseases.

A

GAG

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8
Q

https://drive.google.com/open?id=0B8uJUY-tie8GZ3d6bWRQWlZMR2M

A

https://drive.google.com/open?id=0B8uJUY-tie8GeHlVYUNVek5KclE

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9
Q

https://drive.google.com/open?id=0B8uJUY-tie8GLVg1WUdzS2M5SGc

A

https://drive.google.com/open?id=0B8uJUY-tie8GeWNKR0lSWm03ckU

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10
Q

PG

A

Complex carbohydrates that have a central protein molecule to which

many GAGs are attached in a radial (brush-like) pattern.

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11
Q

PG

A

95% polysaccharide; 5% protein.

■ Linkage of GAGs to the central protein involves a trisaccharide: 2 galactose +

1 xylose.

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12
Q

PG

A

Central protein is rich in serine and threonine

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13
Q

Located mostly in the ECM.

A

PG

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14
Q

A homopolymer of b-D-glucopyranose linked by b-1, 4 bonds.

A

cellulose

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15
Q

Major component of plants.

■ Cannot be digested by humans

A

cellulose

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16
Q

https://drive.google.com/open?id=0B8uJUY-tie8GZHhEWWRzV2p4OTA

A

https://drive.google.com/open?id=0B8uJUY-tie8GZHhEWWRzV2p4OTA

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17
Q

A homopolymer of N-acetyl-D-glucosamine linked by b-1, 4 glycosidic

bonds.

■ Major component of insect and crustacean exoskeletons.

A

chitin

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18
Q

DEXTRAN

A

A homopolymer of glucose formed by the hydrolysis of sucrose via glucosyl

transferase (dextran sucrase).

■ Produced by Streptococcus mutans.

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19
Q

Sucrose —>Fructose + Glucan (Dextran)

A

Glucosyl transferase

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20
Q

LEVAN

A

A homopolymer of fructose formed by the hydrolysis of sucrose via levan

sucrase.

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21
Q

LEvan

A

Increases adhesion of bacteria to tooth surfaces

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22
Q

LEVAN

A

Stored intracellularly as reserve nutrients for bacteri

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23
Q

GLYCOPROTEINS

A

Proteins with covalently linked oligosaccharide (glycan) chains.

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24
Q

GLYCOPROTEINS

A

Function: Structural components, transport molecules, enzymes, receptors,

and hormones.

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25
Q

GP

A

Examples: Collagens, proteoglycans, immunoglobulins, selectins, fibronectin,

laminin, thyroid-stimulating hormone (TSH), and alkaline phosphatase.

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26
Q

GLYCOLIPIDS

A

Sphingolipids with attached carbohydrates

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27
Q

GLYCOLIPIDS

A

Derived from ceramide

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28
Q

glycolipids

A

Commonly found on outer cell membrane surfaces, especially in brain

and other nervous tissues.

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29
Q

glycolipid

A

Examples: Gangliosides, galactosylceramide, and glucosylceramide

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30
Q

saliva

A

A hypotonic fluid with an average pH ranging from 6 to 7.

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31
Q

saliva

A

Salivary duct cells reabsorb Na+/Cl− in exchange for K+/HCO3

−.

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32
Q

saliva

A

Contains mostly water, electrolytes, and organic factors.

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33
Q

Elevated caries risk when salivary flow <——

A

Elevated caries risk when salivary flow <0.7 mL/min.

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34
Q

https://drive.google.com/open?id=0B8uJUY-tie8GRDRvN1k1clFWaEk

A

https://drive.google.com/open?id=0B8uJUY-tie8GNUU2RTFaNWtrYm8

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35
Q

Serous (watery) →

A

contain a-amylase.

36
Q

Mucous (viscous) →

A

contain mucins.

37
Q

https://drive.google.com/open?id=0B8uJUY-tie8GSUxDaWt6RWpOSms

A

https://drive.google.com/open?id=0B8uJUY-tie8GMW1EYmJFZy16OVk

38
Q

SALIVARY CONTROL

A

Controlled by the autonomic nervous system.

39
Q

Parasympathetic action → serous secretions

A

Salivary control

40
Q

Sympathetic action → mucous secret

A

sal. secr.

41
Q

Consist of chains of amino acids (polypeptides), which are arranged in specific

three-dimensional conformations.

A

proteins

42
Q

Building blocks of polypeptides.

■ Basic structure consists of a central a-carbon atom surrounded by four

groups: a hydrogen atom, carboxyl group, amino group, and an R-group

specific to each amino acid.

A

AA

43
Q

All amino acids found in proteins are stereoisomers in the –configuration.

A

All amino acids found in proteins are stereoisomers in the L-configuration.

44
Q

Amino acids are covalently linked by peptide bonds at their amino ((x)

and carboxyl (y) groups

A

Amino acids are covalently linked by peptide bonds at their amino (Nterminus)

and carboxyl (C-terminus) groups

45
Q

peptide bond

A

Generally short, polar, and allow the a-carbon to rotate freely about its

axis (Proline has a restricted a-carbon rotation due to its 3° amine).

46
Q

Generally a trans (not cis) bond

A

PEPTIDE BONDS

47
Q

peptide bond

A

Very stable; generally require proteolytic enzymes to break them.

■ Do not ionize at physiologic pH.

48
Q

https://drive.google.com/open?id=0B8uJUY-tie8Gb0VRdS1adHJSN00

A

https://drive.google.com/open?id=0B8uJUY-tie8GVE93Y2VXSjhOVUk

49
Q

https://drive.google.com/open?id=0B8uJUY-tie8GemRVT3RHNnR3R28

A

https://drive.google.com/open?id=0B8uJUY-tie8GSTkzTl8yUXdlVzg

50
Q

disulfide bond

A

■ Strong, covalent bonds between thiol (–SH) group of two cysteine residues

that stabilizes structure of proteins and prevent denaturation.

51
Q

DISULFIDE BONDS

A

Abundant in insulin and Ig.

52
Q

classification

A

By R-group. (See Table 6–2.)

■ By dietary necessity. (See Table 6–3.)

■ By metabolic end product. (See Table 6–4.)

53
Q

https://drive.google.com/open?id=0B8uJUY-tie8GbTM3cW01azJ1ZG8

A

https://drive.google.com/open?id=0B8uJUY-tie8GazV0dGM2cUxSdGs

54
Q

https://drive.google.com/open?id=0B8uJUY-tie8GYXNla05fUW9BcXc

A

https://drive.google.com/open?id=0B8uJUY-tie8GRWxEbVVfUjZFVzA

55
Q

https://drive.google.com/open?id=0B8uJUY-tie8Geld6eDdKMnh0UkE

A

https://drive.google.com/open?id=0B8uJUY-tie8GbVdWZ0k5ME1uazg

56
Q

Primary structure of AA

A

Primary structure: The specific sequence of amino acids in a polypeptide

chain. Each amino acid in the polypeptide chain is called a residue.

57
Q

Secondary structure:

A

The folding of portions of a polypeptide chain.

58
Q

a-Helix:

A

Coiled configuration.

59
Q

■ b-Pleated sheet: ■

A

Zigzag or pleated configuration.

60
Q

b-Turn:

A

Reverse turns that link two sides of a b-pleated shee

61
Q

Tertiary structure:

A

The overall three-dimensional conformation of a

polypeptide. Each portion of the polypeptide that can perform a biochemical

or physical function is called a domain.

62
Q

Quarternary structure:

A

The spatial arrangement of two or more polypeptide

chains. Each polypeptide is known as a subunit. Associated via noncovalent

interactions.

63
Q

1/3 of body’s protein.

■

A

collagen

64
Q

collagen

A

Consists of three polypeptide a-chains wound around one another to form

a triple helix

65
Q

■ Produced by many cells: fibroblasts, epithelial cells, odontoblasts, osteoblasts,

and chondrocytes

A

collagen

66
Q

It is the organic matrix in dentin and cementum

A

collagen

67
Q

https://drive.google.com/open?id=0B8uJUY-tie8GSFRTRjJwUTFCVmM

A

https://drive.google.com/open?id=0B8uJUY-tie8GdkVPYkZpeGZPLXM

68
Q

COLLAGEN

A

35% glycine; 21% proline; 11% alanine

69
Q

collagne

A

Fibers have high tensile strength

70
Q

rER:

A

Synthesis of a-chains with glycine-x-y sequence

71
Q

rER:

A

Hydroxylation of proline and lysine residues, forming hydroxyproline

and hydroxylysine. Requires vitamin C.

72
Q

Golgi:

A

Glycosylation of α-chains, forming procollagen, a triple helix

containing N- and C-terminal propeptides.

73
Q

Endopeptidases cleave the—– and — terminal propeptides of —–

forming ——

A

Endopeptidases cleave the N- and C-terminal propeptides of procollagen,

forming tropocollagen

74
Q

Cross-linking of —– molecules, forming —– fibrils.

Requires —– of lysine via lysine oxidase (contains copper).

A

Cross-linking of tropocollagen molecules, forming collagen fibrils.

Requires oxidation of lysine via lysine oxidase (contains copper).

75
Q

https://drive.google.com/open?id=0B8uJUY-tie8GekFDYmVVVmlaTXM

A

https://drive.google.com/open?id=0B8uJUY-tie8GSW4xWlhhS1ZuRlk

76
Q

elastin

A

Fibers are extremely elastic, “rubber-like.”

■ Found in skin, ligaments, arterial walls.

77
Q

Synthesis can occur simultaneously with collagen.

A

elastin

78
Q

Elastin

A

Amino acid sequence of the proelastin polypeptide chain is typically

glycine-x-y. Other residues include proline, lysine, alanine, and

hydroxyproline (to a lesser extent).

79
Q

elastin

A

■ Endopeptidases cleave the N- and C-terminal propeptides of proelastin,

forming tropoelastin.

■ Cross-linking of tropoelastin molecules via desmosine, forming elastin

fibers. Requires oxidation of lysine via lysine oxidase (contains copper).

80
Q

plasma protein

A

Synthesized in the liver (except gamma globulins).

■ Act as buffers to stabilize pH.

81
Q

https://drive.google.com/open?id=0B8uJUY-tie8GN0VKMVdFaXBEdzg

A

https://drive.google.com/open?id=0B8uJUY-tie8GQWhzNW5sR3RzYVU

82
Q

Transports O2 in erythrocytes.

A

hemoglobin

83
Q

Each heme reversibly— one molecule of O2 when the iron is in a

——- ferrous (Fe2+) state.

A

Each heme reversibly binds one molecule of O2 when the iron is in a

reduced ferrous (Fe2+) state.

84
Q

Heme binds ——) with a greater affinity than O2.

A

Heme binds carbon monoxide (CO) with a greater affinity than O2.

85
Q

Hb binds ~15% of the CO2 carried inv—— blood (the majority is

carried by —–

A

Hb binds ~15% of the CO2 carried in venous blood (the majority is

carried by bicarbonate).

86
Q

Mutations of a and b subunits result in numerous hemoglobin types.

A

hemoglobin

nbde biochem (14 decks)

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