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MED 110 > 001 Cell Chemistry and Biomolecules > Flashcards

001 Cell Chemistry and Biomolecules Flashcards

1
Q

4 common dietary carbohydrates

A
  1. starch
  2. sucrose
  3. dietary fiber
  4. lactose
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2
Q

nutritional reservoir of CH in plants

A

starch

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3
Q

polysaccharide of glucose

A

starch

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4
Q

the unbranched form of starch

A

amylose (alpha 1,4 glycosidic bonds)

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5
Q

the branched form of starch

A

amylopectin (alpha 1,6 glycosidic bonds)

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6
Q

natural sweetener found in fruits and veggies

A

sucrose

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7
Q

disaccharide of glucose and fructose

A

sucrose

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8
Q

origin of dietary fiber

A

plant origin

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9
Q

major dietary carbohydrates of animal origin

A

lactose

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10
Q

disaccharide of glucose and galactose

A

lactose

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11
Q

three components to help identify a monosaccharide

A
  1. carbon number
  2. functional group (ketone or aldehyde)
  3. stereoisomer form
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12
Q

epimers are called …… that differ in configuration of only one stereogenic (chiral) center

A

diastereomers

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13
Q

the 2 stereoisomer forms

A

D and L

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14
Q

most of the sugars in the human body are in this stereoisomer form

A

D series

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15
Q

alpha anomer

A

OH at C1 is on the opposite side of the ring fro the CH2OH

also the alpha part looks down (hydrogen is up)

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16
Q

beta anomer

A

OH at C1 is on the same side of the ring from the CH2OH

also the beta part goes up (hydrogen is down)

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17
Q

is open chain or the cyclic structure a more stable form?

A

the cyclic form is more stable (most monosaccharides only exist as the ring structure)

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18
Q

5 chemically modified derivatives of monosaccharides

A
  1. deoxyaldose (major component of DNA)
  2. Aceytlated amino sugars ( component of glycoproteins and glycolipids)
  3. acidic sugars (GAGS and proteoglycans)
  4. sugar esters (gangliosides in oligodendrocyte)
  5. sugar alcohols (food additives used in synthesis of lipids)
19
Q

unbranched polymer of glucose joined by beta 1,4 linkages to form long and straight chains

A

cellulose

20
Q

most biologically significant property of all lipid

A

hydrophobic properties

21
Q

fatty acids contain two things

A

1, hydrocarbon chains

2. carboxylic acid group

22
Q

fatty acids are the building blocks of

A

phospholipids and glycolipids (components of membranes)

23
Q

fatty acids synthesized from

A

Acetyl coenzyme A

24
Q

two broad classes of fatty acids

A

fatty acid derivative

isoprenoids

25
Q

these lipids contain multiple units of a five carbon molecule called isoprene

A

isoprenoids

26
Q

three main uses of lipids

A
  1. Fuel stores
  2. structural support
  3. signaling events
27
Q

how many essential amino acids are there

A

10

28
Q

hormones that are produced from amino acids

A

insulin and glucagon

29
Q

in humans most amino acids are in the L-form except

A

D-serine (neurotransmitter)

30
Q

the pKa means the

A

indication of the acidity or the strength of the acidity of the molecule

31
Q

the essential amino acids

A
  1. isoleucine
  2. leucine
  3. methionine
  4. phenylalanine
  5. tryptophan
  6. valine
  7. threonine
  8. arginine
  9. histidine
  10. lysine
32
Q

amino acids contain a ….. acid and its ………. base

A

weak

conjugate

33
Q

henderson hasselbach

A

pH = pK + log ( [A-] / [HA] )

34
Q

when amino acids possess + and - charges at neutral pH

A

zwitterions

35
Q

for amino acids, when the pH is at the charge “zero” it is called the

A

isoelectric point

36
Q

amino acids are converted into two things

A
  1. non-proteinogenic amino acids (non coded or unnatural)

2. biogenic amino acids ( natural and biologically active)

37
Q

proteins are molecules built from amino acids and their three main uses are

A
  1. fuel supply (TCA -> ATP production)
  2. structural support (elastin, collagen)
  3. activity (enzymes, signaling)
38
Q

primary structure proteins

A

linear arrangment
linked to each other by peptide bonds
written as N terminus to C terminus

39
Q

secondary structure proteins

A

created by coiling or pleating of peptide/protein chains
alpha helices
beta pleated sheets
beta turns

40
Q

tertiary structure proteins

A 
3D conformation of specific protein
globular or spherical formation
hydrophobic interactions
disulfide bonds
metal ions
hydrogen bonding
41
Q

two types of tertiary structure of proteins

A 
fibrous proteins (collagen and keratin and water insoluble, roughly parallel fashion, linear)
globular proteins (tightly folded structure like a sphere)
42
Q

the most abundant globular protein in blood

A

serum albumin

43
Q

quaternary protein structure

A 
subunits held together by non covalent associations
hydrogen bonds
salt bridges
hydrophobic interactions
van der waals forces

MED 110 (11 decks)

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