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Molecules 2 People > Amino Acids > Flashcards

Amino Acids Flashcards

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1
Q

The essential amino acids are

A

Phen Alan, Val, and Lucy took Three Trips to Isolate from His Meth Arguments and his Lyce
Phe, val, thr, trp, ile, met, his, arg, leu, lys

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2
Q

Glycine

A

Nonpolar
-H good ol easy glycine

Position 3 of hairpin turn, prevents hindrance with H as R group

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3
Q

Alanine

A

non

-CH3 alan is boring, 1 carbon

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4
Q

Valine

A

non, BCAA

-CH2-CH3-CH3 upside down V for Val

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5
Q

Leucine

A

non, BCAA

-CH2-CH-CH3-CH3 Lucy is like Val, but taller with extra carbon

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6
Q

Isoleucine

A

non, BCAA

Lucy isolates her 4 carbons w single bonds

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7
Q

Proline

A

Non
The pro feline has 3squared lives in a cyclic ring, makes agile turns
Involved position 2 in sharp turn in hairpin loop

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8
Q

Phenylalanine

A

Aromatic, nonpolar

Alan tries to have phen with his new ring

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9
Q

Tyrosine

A

Aromatic, Polar

OH when Alan has phen he gets TYRed

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10
Q

Tryptophan

A

Aromatic, non polar

Don’t trip fam, just a ring on an amine dbl bond

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11
Q

Asparagine

A

Polar, Uncharged

Asparagus Doubles Oxygen, and adds Nitrogen

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12
Q

Glutamine

A

Polar, Uncharged

Lucy is taller than Val, Glutamine is taller than Asparagine

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13
Q

Serine

A

Polar, Uncharged

Alan puts down the ring, and becomes OH so serene

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14
Q

Threonine

A

Polar, Uncharged

Three groups, H, OH, and CH3

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15
Q

Aspartate

A 
Neg charge (acidic)
Part that I hate is that he thinks he COO- or somethin
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16
Q

Glutamate

A 
Neg charge (acidic) 
Mate is taller than Aspartate, still thinks he COO-
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17
Q

Histidine

A

Positive (basic)

“His positivity is great”

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18
Q

Arginine

A

Positive (basic)

Arg, +pirate has a sword of 4 Cs and 3 Ns,

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19
Q

Lysine

A

Positive (basic)

Positive for lice ( 4 C chain with NH3 on end)

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20
Q

Methionine

A

Nonpolar
Sulfur Containing
Susie did meth, now shes surrounded by 3 Crooks

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21
Q

Cysteine

A

Polar
Sulfur Containing
SH, you’re in the cysteine chapel

22
Q

Primary Structure of AAs are held together by what forces

A

Linear sequence with covalent bonds between carbonyl carbons and amide nitrogens (Peptide bond) w R groups in trans position from each other

23
Q

Secondary Structure of AAs and Forces involved

A
  • Alpha Helix stabilized by H bonds, with hydrophilic out and hydrophobic inside
  • Beta pleated Sheet stabilized by H bonds, R groups alternate between above&below plane w bulk hydrophobic core for density
24
Q

Three types of Beta Sheets

A

Parallel-same direction
Anti-Parallel-opposite direction
Mixed- Combo of both

25
Q

What connects different stretches of anti-parallel Beta sheets?

A

Reverse or Hairpin turn, 4 AAs, Stabilized by single H bond between 1st and 4th residue
Proline at 2, Glycine at 3

26
Q

Super-Secondary AA Structures, and Forces Involved

A

Alpha-Alpha Corner, All Beta, and most commonly Beta-Alpha-Beta (BAB) motif
-Stabilized by R group interaction from above the sheet and the outer helix

27
Q

When Beta Alpha Beta motif repeats 7-8 times, It folds into a donut (Alpha-Beta-Barrel) called what, and in what process is this commonly found?

A

Rossmann fold

(Ross loves donuts)

Common among glycolysis enzymes

28
Q

Tertiary Structure of AAs and Forces

A

Final folded state of complete polypeptide, stabilized by hydrophobic interactions, H bonds, Ionic interactions, Disulfide bonds

29
Q

Quaternary Structure of AAs and Forces

A

Multiple polypeptides form supra-molecular complex (di-, tri- meric)
May be identical or different subunits (homo- or hetero-polymeric)

30
Q

Forces Controlling tert and quat AA structures (four)

A

H-bonds, Hydrophobic Forces, Electrostatic forces (charges, dipoles, salt-bridges), Van der Waals Forces(proximity of uncharged non-bonded atoms)

31
Q

Do not contain RNA or DNA, cause neurodegenerative diseases that are from infection (Mad Cow) or Inherited (Creutzfeld-Jakob disease (CJD)

A

Prions (proteinaceous infectious particles)

32
Q

The most abundant protein in body, that provides tensile strength, is formed by what AAs

A

Collagen (Kola=glue)(Pro-Gly)
Formed in triple helix by glycine (fits into small spaces), proline, (kinks polypeptide), and hydroproline&hydroxylysine (stabilize triple helix)

33
Q

What characterizes Scurvy, and why does it occur?

A

Lack of Vit C, which is required to hydroxylate proline and lysine, so triple helix is not stable, and collagen has low tensile strength

34
Q

What characterizes Ehlers-Danlos Sydrome and why does it occur?

A

E-D makes you stretchy, mutation in collagen

35
Q

Osteogenesis Imperfecta (Brittle Bone Disease)

A

Type I collagen formation disruption, mutation may interfere with proper cleaving of end, so stacks of triple helix are misaligned and loose

36
Q

Induced by tobacco smoke elements, which AA has an R-group subject to oxidation?

A

Methionine, which impairs protein function

37
Q

Which AA has R-group subject to spontaneous oxidation that creates disulfide link within protein

A

Cysteine: thiol group

relatively uncommon w intracellular proteins, but common in extracellular proteins (**Insulin has this bond)

38
Q

Isoleucine, Leucine and Valine are increased in what condition?

A

Maple Syrup Urine Disease (MSUD)

39
Q

Phenylketonuria (PKU) is characterized by what?

A

Lack of Phenylalanine hydroxylase, which leads to accumulation of phenylalanine

40
Q

Modified AAs such has 4-hydroxyproline and 5-hydroxylysine are found in what compound?

A

Collagen

41
Q

Blood clotting factors, which involve Ca2+ binding, have which important AAs?

A

Carboxyglutamate, which requires cofactor Vit K which activates the clotting factors

42
Q

How does Vit K deficiency lead to prolonged bleeding and hemorrhage potential?

A

Vit K serves as cofactor in conversion of inactive to active clotting by carboxylation of glutamate

43
Q

Definition of pK and pI

A

pK- prot and unprot exists in approximately equal proportions across all like groups in solution
pI- pH at which molecules possess net charge of 0

44
Q

Which type of AAs form Elastin?

A

Mostly small, nonpolar (gly, alan, val)
Also rich in Proline and Lysine
-Synth from tropoelastin precursor into EC space

45
Q

Amyloidosis is caused by what, and which diseases is it associated with?

A

Accumulation of Amyloid (beta sheet folded into long fiber) protein
-Beta amyloid accum in Alzheimer’s

46
Q

Henderson-Hasselbalch Equation

A

pH=pKa + log (A-)/(HA)

47
Q

Lower the pKa for an acid, the ____ the acid will be

A

stronger (more readily release H+)

48
Q

What can denature proteins?

A
  • Inc or Dec pH
  • Ionic strength changes (salting out)
  • Heating
  • Urea, mercaptoethanol, or guanidine salts that disrupt H-bonds
  • Detergents like sodium dodecyl sulfate (SDS) that disrupts hydrophobic interactions
49
Q

What helps to fold protein into native/functional state?

A

Some spontaneous, some w help of chaperonins.

Chaperones AKA heat shock proteins (HSPs) which increase at high temps

50
Q

Three major properties of proteins that you can separate them with

A

Ion- differences in sign and magnitude of net charge at given pH
Size- w gel filtration
Affinity- Binding specificity to ligand

Molecules 2 People (6 decks)

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