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Medical Biochemistry > Week 1 Content - Intro, Buffers, Acid Base Disorders, AA and Proteins, Hb > Flashcards

Week 1 Content - Intro, Buffers, Acid Base Disorders, AA and Proteins, Hb Flashcards

1
Q

What is considered a volatile acid? How does the body get rid of it?

A

carbon dioxide - major metabolic acid - it is lost in expiration by the lungs

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2
Q

what are the types of non-volatile acids? How does the body get rid of them?

A

Inorganic non-volatile acids = sulfuric acid, phosphoric acid
Organic acids = ketone bodies, lactic acid
All lost through the kidneys and urine

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3
Q

amino acids can act as an acid or a base. What is the name for this?

A

amphoteric

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4
Q

What protein is rich in hisitine side chains?

A

Hb

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5
Q

How is GABA formed? (aa and mechanism)

A

glutamate by decarboxylation

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6
Q

How is histamine formed? (aa and mechanism)

A

histidine by decarboxylation

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7
Q

How is seratonin formed? (aa and mechanism)

A

tryptophan is hydroxylated and decarboxylated

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8
Q

How are catecholamines formed? (aa and mechanism)

A

tyrosine is hydroxylated = L-DOPA

L-DOPA is decarboxylated = dopamine = 1st catecholamine!

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9
Q

peptide bonds are typically…

A

polar and uncharged

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10
Q

denaturing proteins - what breaks hydrogen bonds?

A

heat, urea, salt

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11
Q

denaturing proteins - what breaks ionic bonds?

A

strong acids

strong bases

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12
Q

denaturing proteins - what breaks hyrophobic interactions

A

SDS detergent

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13
Q

denaturing proteins - what breaks/ reduce disulfide bonds?

A

thiol containing compounds
beta mercaptoethanol (Bme)
2-mercaptoethanol

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14
Q

what actually happens in prions disease?

A

PrP = PrPsc
the alpha helix is changed to a beta pleated sheet which is strong
“holes in brain”

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15
Q

myoglobin is a…

A

monomer

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16
Q

hemoglobin is a…

A

tetramer

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17
Q

What fraction of total hemoglobin is Hb A?

A

90% alpha 2 beta 2

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18
Q

what fraction of total hemoglobin is Hb F?

A

< 2%

alpha 2 gamma 2

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19
Q

what fraction of total hemoglobin is Hb A2?

A

2-5%

alpha 2 delta 2

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20
Q

what fraction of total hemoglobin is Hb A1c?

A

3-9%

alpha 2 beta 2 - glucose

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21
Q

what are the negative polar aa?

A

aspartate, glutamate

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22
Q

what are the polar uncharged aa?

A

thrionine, serine, asparagine, glutamine

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23
Q

what are the positively charged polar aa?

A

lysine, arginine, and sometimes histidine!

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24
Q

what factors cause a right shift in the ocygen dissocation curve?

A

decrease O2 affinity = increase in temperature, decrease in pH, increase in PCO2, increase in 2,3 BPG, increase HK, decrease PK
“everything you do with exercise”

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25
with weak acid drugs, what happens if the pH
absorption in stomach = uncharged form!
26
with weak basic drugs, what happens if the pH>pK?
absorption in intestine = uncharged form!
27
what is the primary structure of proteins?
aa sequence
28
what is the secondary structure of proteins?
alpha helix (with hydrogen bond every 4th aa) and beta pleated sheet)
29
what is the tertiary structure of protein?
3D conformation of the protein
30
what is needed for the proper cleavage of insulin?
C-peptide!
31
what do chaparones do in multimeric proteins?
they facilitate proper folding
32
what picks up protein mis folding?
ubiquitin
33
what is the structure common to all amino acids of proteins?
H3C - alpha C - COOH | R side chain (groups i memorized)
34
which polar uncharged aa have an OH group?
serine and thrionine
35
what determines the properties of proteins?
the side chain - structure and function are related
36
what plays an important role in protein folding and function?
polarity of the side chain
37
where do the polar aa cluster (hydrophilic)?
on the surface of soluble proteins
38
where do nonpolar aa cluster (hydrophobic)?
on the surface of membrane proteins
39
how are proteins and peptides synthesized?
translation of mRNA ot protein
40
what are covalent bonds and what are some examples?
they are strong and are not meant to be broken unless during protein degradation peptide bonds between 2 aa disulfide bonds
41
what do non covalent bonds do and what are some examples?
they are weaker and specificy protein folding and conformational changes - these weak forces may be additive hydrophobic forces hydrogen bonds ionic bonds van der walls
42
how are secondary structures of proteins stabilized?
by hydrogen bonds involving the atoms of peptide bonds
43
where are the aa side chains in the alpha helix?
they stick out
44
what is the beta pleated sheet characterized by?
hydrogen bnods perpendicular to peptide bond atoms | aa side chains that alternate above and below plane
45
when can hydrogen bonds be formed?
between 2 polar uncharged side chains | one charged side chain and one polar side chain (ion dipole attractive force)
46
what holds the A and B chains of insulin together?
2 inter-chain disulfide bonds
47
what folds the peptide hormone and is needed for receptor recognition?
the intra-chain disulfide bond
48
what does myoglobin not have?
beta pleasted sheet
49
what is myoglibin describes in terms of?
tertiary structure
50
what is hemoglobin described in terms of?
quaternary structure
51
what in myoglobin and hemoglobin look almost identical?
the beta chain of hemoblogin and the tertiary structure of myoglobin
52
what is monomeric mean?
single polypeptide chain - teritary structure description
53
what does multimeric mean?
more than 1 polypeptide chian - quaternayr structure description
54
what is homomultimeric?
all chains are the same
55
what is heteromultimeric
all chains are different
56
how do the subunits of multimeric proteins (quaternary structure) associate (bonds)
non covalent forces examples - Hb
57
what does HSP 70 do?
prevents aggregation of unfolded prtine
58
what does it mean to denature protien?
3D structure is changed - the peptide backbone is intact - primary structure is good once denatured you can fix it back
59
in alzheimer's disease or prions diseasewhat is the deal with ubiquitin and proteasome?
the diseased proteins are very stable and not picked up - so abnormal proteins accumulate and dammage the brain
60
the infectious agent in prions disese is what?
a single protein
61
what are 3 structual fibrous proteins?
collagen, keratin, elastin
62
what are globular rtansport proteins?
albumin and Hb
63
how are extracellular proteins stabilized?
disulfide bonds - thats why its in albumin
63
how are extracellular proteins stabilized?
disulfide bonds - thats why its in albumin
64
where are hydrophobic forces formed?
between side-chains of branched-chain amino acids. These side chains are nonpolar and they would be normally mainly found inside of a globular protein.
64
where are hydrophobic forces formed?
between side-chains of branched-chain amino acids. These side chains are nonpolar and they would be normally mainly found inside of a globular protein.
65
what does Hsp 60 do?
barrel shape and have function of folding and refolding proteins
65
what does Hsp 60 do?
barrel shape and have function of folding and refolding proteins

Medical Biochemistry (17 decks)

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