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

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

Flashcards in Week 1 Content - Intro, Buffers, Acid Base Disorders, AA and Proteins, Hb Deck (68):
1

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

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

2

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

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

3

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

amphoteric

4

What protein is rich in hisitine side chains?

Hb

5

How is GABA formed? (aa and mechanism)

glutamate by decarboxylation

6

How is histamine formed? (aa and mechanism)

histidine by decarboxylation

7

How is seratonin formed? (aa and mechanism)

tryptophan is hydroxylated and decarboxylated

8

How are catecholamines formed? (aa and mechanism)

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

9

peptide bonds are typically...

polar and uncharged

10

denaturing proteins - what breaks hydrogen bonds?

heat, urea, salt

11

denaturing proteins - what breaks ionic bonds?

strong acids
strong bases

12

denaturing proteins - what breaks hyrophobic interactions

SDS detergent

13

denaturing proteins - what breaks/ reduce disulfide bonds?

thiol containing compounds
beta mercaptoethanol (Bme)
2-mercaptoethanol

14

what actually happens in prions disease?

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

15

myoglobin is a...

monomer

16

hemoglobin is a...

tetramer

17

What fraction of total hemoglobin is Hb A?

90% alpha 2 beta 2

18

what fraction of total hemoglobin is Hb F?

< 2%
alpha 2 gamma 2

19

what fraction of total hemoglobin is Hb A2?

2-5%
alpha 2 delta 2

20

what fraction of total hemoglobin is Hb A1c?

3-9%
alpha 2 beta 2 - glucose

21

what are the negative polar aa?

aspartate, glutamate

22

what are the polar uncharged aa?

thrionine, serine, asparagine, glutamine

23

what are the positively charged polar aa?

lysine, arginine, and sometimes histidine!

24

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

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"

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