Amino Acids and Proteins Flashcards

1
Q

pKa of amino acid carboxylic acid

A

~2.5

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2
Q

pKa of amino acid amino

A

~9.5

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3
Q

Aliphatic AAs

A

Gly, Ala, Leu, Ile, Val

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4
Q

Hydroxyl and Sulfhydrl Containing AAs

A

Ser, Thr, Tyr

Met, Cys, Sec

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5
Q

Acid AAs (and their amides)

A

Asp, Glu

Asn, Gln

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6
Q

Basic AAs

A

Arg, Lys, His

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7
Q

Aromatic AAs and Imino Acid

A

Phe, Tyr, Trp, His

Pro

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8
Q

Wavelength which aromatic amino acids absorb UV light

A

275-280 nm

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9
Q

Strongest chromophore amino acids

A

Tryptophan and tyrosine

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10
Q

Laber-Beer Law

A

A = e c l

e - molar absorptivity constant
c - concentration
l - path length

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11
Q

Angle between atoms on a peptide bond

A

120 degrees

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12
Q

Peptide Bond – trans or cis

A

trans configuration due to steric interference

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13
Q

Physiologically Active Peptides

A

Insulin, glucagon, oxytocin, vasopressin

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14
Q

Glutathione

A

Anti-oxidant preventing damage to cellular components from reactive oxygen species

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15
Q

Glutathione reducase

A

Reduces “disulfide bound glutathione dimer” (terminology?) to 2 glutathione

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16
Q

Glutathione peroxidase

A

Glutathione mediated reduction of hydrogen peroxide by NADPH

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17
Q

Functions of Proteins

A

Enzymes, hormones, storage prteins, transport proteins, structural proteins, protective proteins, contractile proteins

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18
Q

Flavoproteins (what is the prosthetic group?)

A

Flavin nucleotides

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19
Q

Chromoprotein (what is the prosthetic group?)

A

pigmented prosthetic group

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20
Q

Protein purification separating by charge

A

Ion Exchange Chromatography
Isoelectric Focusing
Electrophoresis

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21
Q

Protein purification separating by size

A

Dialysis and Ultracentrifugation
Gel Electrophoresis
Gel Filtration (size exclusion chromatography)

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22
Q

Protein purification separating by charge AND size

A

2D gel

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23
Q

Protein purification separating by specificity

A

affinity chromatography

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24
Q

Protein purification separating by polarity

A

Paper chromatography
Reverse-phase chromatography
Hydrophobic chromatography

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25
Q

Stages of Insulin

A

Preproinsulin -> Proinsulin (lost signal sequence) -> Mature Insulin (lost C peptide)

26
Q

What is phenylisothiocyanate?

A

Edman’s Reagent

27
Q

Two types of MS that work with peptides/proteins

A

Electrospray Ionization (ESI) and Matrix-Assisted Laser Desorption (MALDI)

28
Q

Distance between residues on an alpha helix?

A

3.6 AA

29
Q

Residues which destabilize or disrupt an alpha helix

A

Proline, bulky AAs or like-charged AAs

30
Q

Strong alpha helix formers?

A

Alanine and Leucine (small, hydrophobic)

31
Q

Characteristic of a Type 1 Beta Turn?

A

Proline in 2nd position

32
Q

Characteristic of a Type 2 Beta Turn?

A

Glycine in 3rd position

33
Q

Enzyme responsible for cis-trans conversion of proline

A

proline-cis, trans-isomerase

34
Q

Name of protein responsible for folding viral proteins and also cis-trans isomerase (proline) activity?

A

Cyclophilins

35
Q

Two examples of drugs targeting cyclophilins for viral disease treatment

A

Cyclosporin A and Alisporivir

36
Q

Angle between alpha carbon and amide nitrogen?

A

Phi (ϕ)

37
Q

What is Psi (ψ)?

A

Angle between alpha carbon and carbonyl carbon

38
Q

Diagram predicting protein secondary structure

A

Ramachandran diagram

39
Q

Protein domain definition

A

section of the protein sufficient to perform a particular chemical or physical task (such as binding of a substrate or other ligand)

40
Q

Chaperons

A

responsible for segregating hydrophobic regions of protein into the interior of the protein

41
Q

Heat Shock Proteins

A

Assist with formation of secondary and tertiary structure

42
Q

Protein Disulfide Isomerases

A

Stabilize tertiary and quaternary structures of proteins, forming a mature conformation

43
Q

Proteolytic Pathways in Eukaryotes

A
  • Endosome-lysosome pathway (extracellular and cell surface proteins)
  • Ubiquitin-proteasome pathway (cytoplasmic, nuclear, and ER proteins)
  • Mitochondria have their own
44
Q

Greater than 10 axial ratio makes a protein….

A

Fibrous

45
Q

Collagen has two post-translationally modified residues

A

hydroxyPro and hydroxyLys

46
Q

HydroxyLys and HydroxyPro are responsible for….

A

cross-linking in collagen

47
Q

Names of fibrillar collagen synthesizing cells for respective locations: loose connective tissue, bone, and cartilage

A

Fibroblasts, osteoblasts, chondroblasts

48
Q

Which residue can be glycosylated in collagen?

A

HydroxyLys

49
Q

What cofactors does prolyl hydroxylase require?

A

alpha-KG, oxygen, Iron (II), and Ascorbate (Vit C)

50
Q

What is Vitamin C’s other name?

A

Ascorbate

51
Q

Symptoms of scurvy?

A

Bruise-like skin discolorations and gum/teeth problems. Caused by weak collagen cross-links

52
Q

Lysyl oxidase does what?

A

catalyzes cross-linking in collagen fibrils

53
Q

Copper (II) deficiency for Lysyl oxidase is called what?

A

Menkes Disease. Leads to brittle hair!

54
Q

Inhibitor of lysl oxidase

A

Sweet pea.

Condition is lathyrism, characterized by skeletal and vascular problems

55
Q

Ehlers-Danlos Syndrome

A

Connective tissue disorders resulting from heritable defects in fibrillar collagen metabolism

56
Q

Osteogenesis Imperfecta

A

Aka brittle bone disease.

Genetic disorder of bone fragility characterized by bones that fracture easily.

57
Q

What protein is found in lungs, arteries, elastic ligaments, skin and the baldder. (Hint: in the arteries its a medium of pressure wave propagation to help blood flow)

A

Elastin

58
Q

What inhibits elastase?

A

alpha-1 antitrypsin

59
Q

Alpha-1 Antrypsin Deficiency

A

basically COPD. Lungs not protected from neutrophil elastase.

60
Q

Smoking’s effect on the lungs

A

It inactivates alpha-1 antitrypsin by oxidizing Methionine residues (351 and 358)

61
Q

SERPINA1 Deficiency

A

Alpha-1 Antritrypsin deficiency. Common among NA and Europeans. Two ZZ genes will cause it.

62
Q

What is it called when a protein has non-Amino Acid components?

A

conjugated protein