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

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
these lipids contain multiple units of a five carbon molecule called isoprene
isoprenoids
26
three main uses of lipids
1. Fuel stores 2. structural support 3. signaling events
27
how many essential amino acids are there
10
28
hormones that are produced from amino acids
insulin and glucagon
29
in humans most amino acids are in the L-form except
D-serine (neurotransmitter)
30
the pKa means the
indication of the acidity or the strength of the acidity of the molecule
31
the essential amino acids
1. isoleucine 2. leucine 3. methionine 4. phenylalanine 5. tryptophan 6. valine 7. threonine 8. arginine 9. histidine 10. lysine
32
amino acids contain a ..... acid and its .......... base
weak | conjugate
33
henderson hasselbach
pH = pK + log ( [A-] / [HA] )
34
when amino acids possess + and - charges at neutral pH
zwitterions
35
for amino acids, when the pH is at the charge "zero" it is called the
isoelectric point
36
amino acids are converted into two things
1. non-proteinogenic amino acids (non coded or unnatural) | 2. biogenic amino acids ( natural and biologically active)
37
proteins are molecules built from amino acids and their three main uses are
1. fuel supply (TCA -> ATP production) 2. structural support (elastin, collagen) 3. activity (enzymes, signaling)
38
primary structure proteins
linear arrangment linked to each other by peptide bonds written as N terminus to C terminus
39
secondary structure proteins
created by coiling or pleating of peptide/protein chains alpha helices beta pleated sheets beta turns
40
tertiary structure proteins
``` 3D conformation of specific protein globular or spherical formation hydrophobic interactions disulfide bonds metal ions hydrogen bonding ```
41
two types of tertiary structure of proteins
``` fibrous proteins (collagen and keratin and water insoluble, roughly parallel fashion, linear) globular proteins (tightly folded structure like a sphere) ```
42
the most abundant globular protein in blood
serum albumin
43
quaternary protein structure
``` subunits held together by non covalent associations hydrogen bonds salt bridges hydrophobic interactions van der waals forces ```