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Elements of Medicine > Amino Acids and Proteins > Flashcards

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
Stages of Insulin
Preproinsulin -> Proinsulin (lost signal sequence) -> Mature Insulin (lost C peptide)
26
What is phenylisothiocyanate?
Edman's Reagent
27
Two types of MS that work with peptides/proteins
Electrospray Ionization (ESI) and Matrix-Assisted Laser Desorption (MALDI)
28
Distance between residues on an alpha helix?
3.6 AA
29
Residues which destabilize or disrupt an alpha helix
Proline, bulky AAs or like-charged AAs
30
Strong alpha helix formers?
Alanine and Leucine (small, hydrophobic)
31
Characteristic of a Type 1 Beta Turn?
Proline in 2nd position
32
Characteristic of a Type 2 Beta Turn?
Glycine in 3rd position
33
Enzyme responsible for cis-trans conversion of proline
proline-cis, trans-isomerase
34
Name of protein responsible for folding viral proteins and also cis-trans isomerase (proline) activity?
Cyclophilins
35
Two examples of drugs targeting cyclophilins for viral disease treatment
Cyclosporin A and Alisporivir
36
Angle between alpha carbon and amide nitrogen?
Phi (ϕ)
37
What is Psi (ψ)?
Angle between alpha carbon and carbonyl carbon
38
Diagram predicting protein secondary structure
Ramachandran diagram
39
Protein domain definition
section of the protein sufficient to perform a particular chemical or physical task (such as binding of a substrate or other ligand)
40
Chaperons
responsible for segregating hydrophobic regions of protein into the interior of the protein
41
Heat Shock Proteins
Assist with formation of secondary and tertiary structure
42
Protein Disulfide Isomerases
Stabilize tertiary and quaternary structures of proteins, forming a mature conformation
43
Proteolytic Pathways in Eukaryotes
* Endosome-lysosome pathway (extracellular and cell surface proteins) * Ubiquitin-proteasome pathway (cytoplasmic, nuclear, and ER proteins) * Mitochondria have their own
44
Greater than 10 axial ratio makes a protein....
Fibrous
45
Collagen has two post-translationally modified residues
hydroxyPro and hydroxyLys
46
HydroxyLys and HydroxyPro are responsible for....
cross-linking in collagen
47
Names of fibrillar collagen synthesizing cells for respective locations: loose connective tissue, bone, and cartilage
Fibroblasts, osteoblasts, chondroblasts
48
Which residue can be glycosylated in collagen?
HydroxyLys
49
What cofactors does prolyl hydroxylase require?
alpha-KG, oxygen, Iron (II), and Ascorbate (Vit C)
50
What is Vitamin C's other name?
Ascorbate
51
Symptoms of scurvy?
Bruise-like skin discolorations and gum/teeth problems. Caused by weak collagen cross-links
52
Lysyl oxidase does what?
catalyzes cross-linking in collagen fibrils
53
Copper (II) deficiency for Lysyl oxidase is called what?
Menkes Disease. Leads to brittle hair!
54
Inhibitor of lysl oxidase
Sweet pea. Condition is lathyrism, characterized by skeletal and vascular problems
55
Ehlers-Danlos Syndrome
Connective tissue disorders resulting from heritable defects in fibrillar collagen metabolism
56
Osteogenesis Imperfecta
Aka brittle bone disease. Genetic disorder of bone fragility characterized by bones that fracture easily.
57
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)
Elastin
58
What inhibits elastase?
alpha-1 antitrypsin
59
Alpha-1 Antrypsin Deficiency
basically COPD. Lungs not protected from neutrophil elastase.
60
Smoking's effect on the lungs
It inactivates alpha-1 antitrypsin by oxidizing Methionine residues (351 and 358)
61
SERPINA1 Deficiency
Alpha-1 Antritrypsin deficiency. Common among NA and Europeans. Two ZZ genes will cause it.
62
What is it called when a protein has non-Amino Acid components?
conjugated protein

Elements of Medicine (8 decks)

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