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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

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USMLE® Step 1 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
Q

with weak acid drugs, what happens if the pH<pK?

A

absorption in stomach = uncharged form!

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26
Q

with weak basic drugs, what happens if the pH>pK?

A

absorption in intestine = uncharged form!

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27
Q

what is the primary structure of proteins?

A

aa sequence

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28
Q

what is the secondary structure of proteins?

A

alpha helix (with hydrogen bond every 4th aa) and beta pleated sheet)

29
Q

what is the tertiary structure of protein?

A

3D conformation of the protein

30
Q

what is needed for the proper cleavage of insulin?

A

C-peptide!

31
Q

what do chaparones do in multimeric proteins?

A

they facilitate proper folding

32
Q

what picks up protein mis folding?

A

ubiquitin

33
Q

what is the structure common to all amino acids of proteins?

A

H3C - alpha C - COOH
|
R side chain (groups i memorized)

34
Q

which polar uncharged aa have an OH group?

A

serine and thrionine

35
Q

what determines the properties of proteins?

A

the side chain - structure and function are related

36
Q

what plays an important role in protein folding and function?

A

polarity of the side chain

37
Q

where do the polar aa cluster (hydrophilic)?

A

on the surface of soluble proteins

38
Q

where do nonpolar aa cluster (hydrophobic)?

A

on the surface of membrane proteins

39
Q

how are proteins and peptides synthesized?

A

translation of mRNA ot protein

40
Q

what are covalent bonds and what are some examples?

A

they are strong and are not meant to be broken unless during protein degradation

peptide bonds between 2 aa
disulfide bonds

41
Q

what do non covalent bonds do and what are some examples?

A

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
Q

how are secondary structures of proteins stabilized?

A

by hydrogen bonds involving the atoms of peptide bonds

43
Q

where are the aa side chains in the alpha helix?

A

they stick out

44
Q

what is the beta pleated sheet characterized by?

A

hydrogen bnods perpendicular to peptide bond atoms

aa side chains that alternate above and below plane

45
Q

when can hydrogen bonds be formed?

A

between 2 polar uncharged side chains

one charged side chain and one polar side chain (ion dipole attractive force)

46
Q

what holds the A and B chains of insulin together?

A

2 inter-chain disulfide bonds

47
Q

what folds the peptide hormone and is needed for receptor recognition?

A

the intra-chain disulfide bond

48
Q

what does myoglobin not have?

A

beta pleasted sheet

49
Q

what is myoglibin describes in terms of?

A

tertiary structure

50
Q

what is hemoglobin described in terms of?

A

quaternary structure

51
Q

what in myoglobin and hemoglobin look almost identical?

A

the beta chain of hemoblogin and the tertiary structure of myoglobin

52
Q

what is monomeric mean?

A

single polypeptide chain - teritary structure description

53
Q

what does multimeric mean?

A

more than 1 polypeptide chian - quaternayr structure description

54
Q

what is homomultimeric?

A

all chains are the same

55
Q

what is heteromultimeric

A

all chains are different

56
Q

how do the subunits of multimeric proteins (quaternary structure) associate (bonds)

A

non covalent forces

examples - Hb

57
Q

what does HSP 70 do?

A

prevents aggregation of unfolded prtine

58
Q

what does it mean to denature protien?

A

3D structure is changed - the peptide backbone is intact - primary structure is good

once denatured you can fix it back

59
Q

in alzheimer’s disease or prions diseasewhat is the deal with ubiquitin and proteasome?

A

the diseased proteins are very stable and not picked up - so abnormal proteins accumulate and dammage the brain

60
Q

the infectious agent in prions disese is what?

A

a single protein

61
Q

what are 3 structual fibrous proteins?

A

collagen, keratin, elastin

62
Q

what are globular rtansport proteins?

A

albumin and Hb

63
Q

how are extracellular proteins stabilized?

A

disulfide bonds - thats why its in albumin

63
Q

how are extracellular proteins stabilized?

A

disulfide bonds - thats why its in albumin

64
Q

where are hydrophobic forces formed?

A

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
Q

where are hydrophobic forces formed?

A

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
Q

what does Hsp 60 do?

A

barrel shape and have function of folding and refolding proteins

65
Q

what does Hsp 60 do?

A

barrel shape and have function of folding and refolding proteins

Medical Biochemistry (17 decks)

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