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MCM - Molecular and Cellular Mechanisms) > TBL 1 - Amino acids and structure function relationships in proteins > Flashcards

TBL 1 - Amino acids and structure function relationships in proteins Flashcards

1
Q

Amino acid configuration found in proteins in the human body

A

L

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2
Q

L-DOPA

A

Derivative of tyrosine

Used to treat Parkinson’s disease

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3
Q

Essential Amino acids

A

THIK WLF VRM

Threonine
Histidine
Isoleucine
Lysine
Tryptophan
Leucine
Phenylalanine
Valine
Arginine - Essential in growing children
Methionine
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4
Q

Gylcine is:

A

Flexible

Achiral

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5
Q

AA which is used as a source of energy for muscles

A

Alanine

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6
Q

SAM

A

S-adenosyl methionine

Methyl donor

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7
Q

BCAA’s

A

Isoeucine
Leucine
Valine

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8
Q

MSUD

A

Maple syrup urine disease

Deficiency in alpha-ketoacid dehydrogenase complex

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9
Q

PKU

A

Phenylketonuria

Deficiency in phenylalanine hydroxylase

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10
Q

Which AA makes tyrosine? and by using which enzyme?

A

Phenylalanine

Phenylalanine hydroxylase

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11
Q

Precursor of DOPA

A

Tyrosine

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12
Q

Ketogenic only AA’s

A

KiLL

Lysine
Leucine

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13
Q

Gucogenic and ketogenic AA’s

A

Isoleucine, phenylalanine, threonine, tyrosine, tryptophan

Thank You IF u Would

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14
Q

Basic AA’s
vs
Acidic AA’s

A

Arginine
Lysine
Histidine

Aspartic acid
Glutamic acid

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15
Q

AA which is neutral at physiological pH:

A

Histidine

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16
Q

2 modified AA’s, how they are made and their biochemical significance:

A

hydroxyproline hydroxylysine

Hydroxylation reaction which requires Vitamin C as a cofactor

Used in collagen production

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17
Q

MSUD causes:

A

A build up of BCAAs in urine, and blood which are toxic to the brain and cause mental retardation

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18
Q

PKU patients can not synthesize which AA?

A

Tyrosine

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19
Q

Melanin is created by which AA

A

Tyrosine

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20
Q

In a PKU patient, phenylalanine is converted to what? and why

A

it can not be converted to tyrosine due the absence of phenylalanine hydroxylase, so instead it is converted to phenylacetate and phenyllacetate

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21
Q

Presentation of PKU patient

A

Mental retardation
Musty odor to urine
Hypopigmentation to skin

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22
Q

Serine and tyrosine unergo _____ reaction at the _____ group

A

phosphorylation

hydroxyl

23
Q

AA’s that modify the acitivites of many enzymes through phosphorylation

A

Serine and tyrosine

24
Q

Tyrosine is the precursor for:

A

Tyrosine Doesn’t Need Everyone To Make Dopamine

DOPA, norepinephrine, epinephrine, thyroxine, melanin, dopamine

25
Q

Tryptophan is the precursor for:

A

Tryp’n Never helped a Medical Student

niacin (B3), melatonin, serotonin

26
Q

Glutamine carries ______

A

Ammonia through out the body

27
Q

Methionine is crucial in:

A

MET - STARTing the polypeptide chain
Synthesis of methyl donor SAM (S-adenosyl methionine)

Have you ever MET SAM?

28
Q

Glycine’s importance:

A

Heme production

Abundant in collagen

29
Q

Bonding present in secondary structures

A 
Hydrogen bonding (intramolecular for alpha-helix intermolecular for beta-sheets)
Sometimes disulfide bonding
30
Q

Amino acids that are largely apart of alpha helices and why

A

Glycine- flexibility

Proline- rdigidity

31
Q

3 types of beta sheets:

A

parallel, antiparallel, mixed

32
Q

How are beta sheets connected?

A

Beta-turns which consist of proline and glycine

33
Q

Beta turns frequently connect:

A

antiparallel beta-sheets

34
Q

Motifs aka

A

super secondary structure

35
Q

What are motifs:

A

Commonly observed folding motifs comprised of different secondary structures

36
Q

______ have the characteristics of a small compact globular protein that is independent of other ____

A

Domain(s)

37
Q

Domains can consist of which protein structure type

A

Tertiary structure

38
Q

4 stabilizing interactions in protein folding

A

Ionic or electrostatic
Hydrogen bonding
DIsulfide bonding
Hydrophobic interactions

39
Q

Quaternary structures are stabilized by:

A

non-covalent interactions

40
Q

_____ assist in the proper folding of proteins

A

Chaperones

41
Q

Mercaptethanol with Urea

A

Added to protein to break disulfide bonds / unfold protein structure

Reversible

42
Q

Abnormal protein in sickle cell anemia

A

β-globin

43
Q

Abnormal protein in Alzheimers disease

A

β-amyloid

44
Q

Abnormal protein in CJD/Kuru/Mad cow

A

Prions

45
Q

Abnormal protein in Huntingtons disease

A

polyglutamine repeats

46
Q

Abnormal protein in parkinsons disease
and
Characteristic finding:

A

α-synuclein

Lewy bodies

47
Q

Abnormal protein in osteogenesis imperfecta

A

Collagen type I

48
Q

Abnormal protein in Elhers-danlos syndrome

A

Collagen type III

49
Q

Protein denatruation caused by:

A

Increasing or decreasing pH
Altering ionic strength
Increasign temperature
Denaturing agents (SDS, Mercaptoethanol, urea)

50
Q

Fibrous protein

A

Insoluable in water
Elongated and ridgid conformation
Structural
Ex: collagen and elastin

51
Q

Collagen provides ______ strength

A

Tensile

52
Q

Collagen is comprised of:

A

Glycine, proline, hydroxyproline and hydroxylysine

53
Q

Parkinsons disease is characterized by a loss of conversion of ________ to ________

A

DOPA to Dopamine

54
Q

Vitamin C deficiency leads to:

A

Scurvy - abnormal integrity of connective tissue and skin, leads to easy bruising

MCM - Molecular and Cellular Mechanisms) (6 decks)

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